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242 results on '"Janssen, Bert J. C."'

5. Contactin 2 homophilic adhesion structure and conformational plasticity

Author

Chataigner, Lucas M P, Thärichen, Lena, Beugelink, J Wouter, Granneman, Joke C M, Mokiem, Nadia J, Snijder, Joost, Förster, Friedrich, Janssen, Bert J C, Chataigner, Lucas M P, Thärichen, Lena, Beugelink, J Wouter, Granneman, Joke C M, Mokiem, Nadia J, Snijder, Joost, Förster, Friedrich, and Janssen, Bert J C

Abstract

The cell-surface attached glycoprotein contactin 2 is ubiquitously expressed in the nervous system and mediates homotypic cell-cell interactions to organize cell guidance, differentiation, and adhesion. Contactin 2 consists of six Ig and four fibronectin type III domains (FnIII) of which the first four Ig domains form a horseshoe structure important for homodimerization and oligomerization. Here we report the crystal structure of the six-domain contactin 2 Ig1-6 and show that the Ig5-Ig6 combination is oriented away from the horseshoe with flexion in interdomain connections. Two distinct dimer states, through Ig1-Ig2 and Ig3-Ig6 interactions, together allow formation of larger oligomers. Combined size exclusion chromatography with multiangle light scattering (SEC-MALS), small-angle X-ray scattering (SAXS) and native MS analysis indicates contactin 2 Ig1-6 oligomerizes in a glycan dependent manner. SAXS and negative-stain electron microscopy reveals inherent plasticity of the contactin 2 full-ectodomain. The combination of intermolecular binding sites and ectodomain plasticity explains how contactin 2 can function as a homotypic adhesion molecule in diverse intercellular environments.

Published
2024

6. Structural Basis for Recognition of the FLAG-tag by Anti-FLAG M2

Author

Beugelink, J. Wouter, Sweep, Els, Janssen, Bert J. C., Snijder, Joost, Pronker, Matti F., Beugelink, J. Wouter, Sweep, Els, Janssen, Bert J. C., Snijder, Joost, and Pronker, Matti F.

Abstract

The FLAG-tag/anti-FLAG system is a widely used biochemical tool for protein detection and purification. Anti-FLAG M2 is the most popular antibody against the FLAG-tag, due to its ease of use, versatility, and availability in pure form or as bead conjugate. M2 binds N-terminal, C-terminal and internal FLAG-tags and binding is calcium-independent, but the molecular basis for the FLAG-tag specificity and recognition remains unresolved. Here we present an atomic resolution (1.17 Å) structure of the FLAG peptide in complex with the Fab of anti-FLAG M2, revealing key binding determinants. Five of the eight FLAG peptide residues form direct interactions with paratope residues. The FLAG peptide adopts a 310 helix conformation in complex with the Fab. These structural insights allowed us to rationally introduce point mutations on both the peptide and antibody side. We tested these by surface plasmon resonance, leading us to propose a shorter yet equally binding version of the FLAG-tag for the M2 antibody.

Published
2024

7. Contactin 2 homophilic adhesion structure and conformational plasticity

Author

Sub Structural Biochemistry, Sub Biomol.Mass Spectrometry & Proteom., Chataigner, Lucas M P, Thärichen, Lena, Beugelink, J Wouter, Granneman, Joke C M, Mokiem, Nadia J, Snijder, Joost, Förster, Friedrich, Janssen, Bert J C, Sub Structural Biochemistry, Sub Biomol.Mass Spectrometry & Proteom., Chataigner, Lucas M P, Thärichen, Lena, Beugelink, J Wouter, Granneman, Joke C M, Mokiem, Nadia J, Snijder, Joost, Förster, Friedrich, and Janssen, Bert J C

Published
2024

12. Mechanistic insights into the C55-P targeting lipopeptide antibiotics revealed by structure-activity studies and high-resolution crystal structures

Author

Wood, Thomas M., Zeronian, Matthieu R., Buijs, Ned, Bertheussen, Kristine, Abedian, Hanieh K., Johnson, Aidan V., Pearce, Nicholas M., Lutz, Martin, Kemmink, Johan, Seirsma, Tjalling, Hamoen, Leendert W., Janssen, Bert J. C., Martin, Nathaniel I., Afd Chemical Biology and Drug Discovery, Sub Structural Biochemistry, Structural Biochemistry, Pharmacology, Afd Chemical Biology and Drug Discovery, Sub Structural Biochemistry, Structural Biochemistry, Pharmacology, Stratingh Institute of Chemistry, and Bacterial Cell Biology & Physiology (SILS, FNWI)

Subjects
General Chemistry
Abstract

The continued rise of antibiotic resistance is a global concern that threatens to undermine many aspects of modern medical practice. Key to addressing this threat is the discovery and development of new antibiotics that operate by unexploited modes of action. The so-called calcium-dependent lipopeptide antibiotics (CDAs) are an important emerging class of natural products that provides a source of new antibiotic agents rich in structural and mechanistic diversity. Notable in this regard is the subset of CDAs comprising the laspartomycins and amphomycins/friulimicins that specifically target the bacterial cell wall precursor undecaprenyl phosphate (C55-P). In this study we describe the design and synthesis of new C55-P-targeting CDAs with structural features drawn from both the laspartomycin and amphomycin/friulimicin classes. Assessment of these lipopeptides revealed previously unknown and surprisingly subtle structural features that are required for antibacterial activity. High-resolution crystal structures further indicate that the amphomycin/friulimicin-like lipopeptides adopt a unique crystal packing that governs their interaction with C55-P and provides an explanation for their antibacterial effect. In addition, live-cell microscopy studies provide further insights into the biological activity of the C55-P targeting CDAs highlighting their unique mechanism of action relative to the clinically used CDA daptomycin.

Published
2022

14. Structural insights into the contactin 1 - neurofascin 155 adhesion complex

Author

Chataigner, Lucas M P, Gogou, Christos, den Boer, Maurits A, Frias, Cátia P, Thies-Weesie, Dominique M E, Granneman, Joke C M, Heck, Albert J R, Meijer, Dimphna H, Janssen, Bert J C, Chataigner, Lucas M P, Gogou, Christos, den Boer, Maurits A, Frias, Cátia P, Thies-Weesie, Dominique M E, Granneman, Joke C M, Heck, Albert J R, Meijer, Dimphna H, and Janssen, Bert J C

Abstract

Cell-surface expressed contactin 1 and neurofascin 155 control wiring of the nervous system and interact across cells to form and maintain paranodal myelin-axon junctions. The molecular mechanism of contactin 1 - neurofascin 155 adhesion complex formation is unresolved. Crystallographic structures of complexed and individual contactin 1 and neurofascin 155 binding regions presented here, provide a rich picture of how competing and complementary interfaces, post-translational glycosylation, splice differences and structural plasticity enable formation of diverse adhesion sites. Structural, biophysical, and cell-clustering analysis reveal how conserved Ig1-2 interfaces form competing heterophilic contactin 1 - neurofascin 155 and homophilic neurofascin 155 complexes whereas contactin 1 forms low-affinity clusters through interfaces on Ig3-6. The structures explain how the heterophilic Ig1-Ig4 horseshoe's in the contactin 1 - neurofascin 155 complex define the 7.4 nm paranodal spacing and how the remaining six domains enable bridging of distinct intercellular distances.

Published
2022

15. Structural insights into the contactin 1 - neurofascin 155 adhesion complex

Author

Sub Structural Biochemistry, Sub Biomol.Mass Spectrometry & Proteom., Sub Physical and Colloid Chemistry, Afd Biomol.Mass Spect. and Proteomics, Structural Biochemistry, Physical and Colloid Chemistry, Biomolecular Mass Spectrometry and Proteomics, Chataigner, Lucas M P, Gogou, Christos, den Boer, Maurits A, Frias, Cátia P, Thies-Weesie, Dominique M E, Granneman, Joke C M, Heck, Albert J R, Meijer, Dimphna H, Janssen, Bert J C, Sub Structural Biochemistry, Sub Biomol.Mass Spectrometry & Proteom., Sub Physical and Colloid Chemistry, Afd Biomol.Mass Spect. and Proteomics, Structural Biochemistry, Physical and Colloid Chemistry, Biomolecular Mass Spectrometry and Proteomics, Chataigner, Lucas M P, Gogou, Christos, den Boer, Maurits A, Frias, Cátia P, Thies-Weesie, Dominique M E, Granneman, Joke C M, Heck, Albert J R, Meijer, Dimphna H, and Janssen, Bert J C

Published
2022

16. Teneurin4 dimer structures reveal a calcium-stabilized compact conformation supporting homomeric trans-interactions

Author

Sub Crystal and Structural Chemistry, Sub Structural Biochemistry, Structural Biochemistry, Meijer, Dimphna H, Frias, Cátia P, Beugelink, J Wouter, Deurloo, Yanthi N, Janssen, Bert J C, Sub Crystal and Structural Chemistry, Sub Structural Biochemistry, Structural Biochemistry, Meijer, Dimphna H, Frias, Cátia P, Beugelink, J Wouter, Deurloo, Yanthi N, and Janssen, Bert J C

Published
2022

17. Structural insights into the non-inhibitory mechanism of the anti-EGFR EgB4 nanobody

Author

Sub Structural Biochemistry, Sub Cell Biology, Celbiologie, Structural Biochemistry, Zeronian, Matthieu R., Doulkeridou, Sofia, Van bergen en henegouwen, Paul M. P., Janssen, Bert J. C., Sub Structural Biochemistry, Sub Cell Biology, Celbiologie, Structural Biochemistry, Zeronian, Matthieu R., Doulkeridou, Sofia, Van bergen en henegouwen, Paul M. P., and Janssen, Bert J. C.

Published
2022

18. Mechanistic insights into the C55-P targeting lipopeptide antibiotics revealed by structure–activity studies and high-resolution crystal structures†

Author

Afd Chemical Biology and Drug Discovery, Sub Structural Biochemistry, Structural Biochemistry, Pharmacology, Wood, Thomas M., Zeronian, Matthieu R., Buijs, Ned, Bertheussen, Kristine, Abedian, Hanieh K., Johnson, Aidan V., Pearce, Nicholas M., Lutz, Martin, Kemmink, Johan, Seirsma, Tjalling, Hamoen, Leendert W., Janssen, Bert J. C., Martin, Nathaniel I., Afd Chemical Biology and Drug Discovery, Sub Structural Biochemistry, Structural Biochemistry, Pharmacology, Wood, Thomas M., Zeronian, Matthieu R., Buijs, Ned, Bertheussen, Kristine, Abedian, Hanieh K., Johnson, Aidan V., Pearce, Nicholas M., Lutz, Martin, Kemmink, Johan, Seirsma, Tjalling, Hamoen, Leendert W., Janssen, Bert J. C., and Martin, Nathaniel I.

Published
2022

20. Internalization and Transport of PEGylated Lipid-Based Mixed Micelles across Caco-2 Cells Mediated by Scavenger Receptor B1

Author

Su, Xiangjie, primary, Ramírez-Escudero, Mercedes, additional, Sun, Feilong, additional, van den Dikkenberg, Joep B., additional, van Steenbergen, Mies J., additional, Pieters, Roland J., additional, Janssen, Bert J. C., additional, van Hasselt, Peter M., additional, Hennink, Wim E., additional, and van Nostrum, Cornelus F., additional

Published
2021
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24. Structural Perspectives on Extracellular Recognition and Conformational Changes of Several Type-I Transmembrane Receptors

Author

Chataigner, Lucas M P, Leloup, Nadia, Janssen, Bert J C, Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry, Crystal and Structural Chemistry, and Sub Crystal and Structural Chemistry

Subjects
0301 basic medicine, Cell signaling, Review, Biochemistry, Genetics and Molecular Biology (miscellaneous), Biochemistry, 03 medical and health sciences, 0302 clinical medicine, Cell surface receptor, Extracellular, cell signaling, rearrangements, Molecular Biosciences, Cell adhesion, Molecular Biology, lcsh:QH301-705.5, Chemistry, interactions, structures, Transmembrane protein, Cell biology, transmembrane, Transmembrane domain, Cytosol, 030104 developmental biology, lcsh:Biology (General), 030220 oncology & carcinogenesis, conformations, Intracellular
Abstract

Type-I transmembrane proteins represent a large group of 1,412 proteins in humans with a multitude of functions in cells and tissues. They are characterized by an extracellular, or luminal, N-terminus followed by a single transmembrane helix and a cytosolic C-terminus. The domain composition and structures of the extracellular and intercellular segments differ substantially amongst its members. Most of the type-I transmembrane proteins have roles in cell signaling processes, as ligands or receptors, and in cellular adhesion. The extracellular segment often determines specificity and can control signaling and adhesion. Here we focus on recent structural understanding on how the extracellular segments of several diverse type-I transmembrane proteins engage in interactions and can undergo conformational changes for their function. Interactions at the extracellular side by proteins on the same cell or between cells are enhanced by the transmembrane setting. Extracellular conformational domain rearrangement and structural changes within domains alter the properties of the proteins and are used to regulate signaling events. The combination of structural properties and interactions can support the formation of larger-order assemblies on the membrane surface that are important for cellular adhesion and intercellular signaling.

Published
2020

25. Structural characterization of anti-CCL5 activity of the tick salivary protein evasin-4

Author

Sub Crystal and Structural Chemistry, Crystal and Structural Chemistry, Denisov, Stepan S, Ramírez-Escudero, Mercedes, Heinzmann, Alexandra C A, Ippel, Johannes H, Dawson, Philip E, Koenen, Rory R, Hackeng, Tilman M, Janssen, Bert J C, Dijkgraaf, Ingrid, Sub Crystal and Structural Chemistry, Crystal and Structural Chemistry, Denisov, Stepan S, Ramírez-Escudero, Mercedes, Heinzmann, Alexandra C A, Ippel, Johannes H, Dawson, Philip E, Koenen, Rory R, Hackeng, Tilman M, Janssen, Bert J C, and Dijkgraaf, Ingrid

Published
2020

27. Structures of complement component C3 provide insights into the function and evolution of immunity

Author

Janssen, Bert J. C., Huizinga, Eric G., Raaijmakers, Hans C. A., Roos, Anja, Daha, Mohamed R., Nilsson-Ekdahl, Kristina, Nilsson, Bo, and Gros, Piet

Subjects
Environmental issues, Science and technology, Zoology and wildlife conservation
Abstract

Author(s): Bert J. C. Janssen [1]; Eric G. Huizinga [1]; Hans C. A. Raaijmakers [1]; Anja Roos [2]; Mohamed R. Daha [2]; Kristina Nilsson-Ekdahl [3, 4]; Bo Nilsson [3]; Piet [...]

Published
2005
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30. Teneurin structures are composed of ancient bacterial protein domains

Author

Jackson, Verity A., Busby, Jason N., Janssen, Bert J. C., Lott, J. Shaun, Seiradake, Elena, Sub Crystal and Structural Chemistry, Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry, and Crystal and Structural Chemistry

Subjects
Teneurin, 0303 health sciences, Microbial toxins, 030306 microbiology, General Neuroscience, Alternative splicing, cell adhesion, Computational biology, Review, Biology, biology.organism_classification, lcsh:RC321-571, Bacterial protein, 03 medical and health sciences, Data sequences, evolution, biology.protein, bacterial toxin, teneurin, Choanoflagellate, lcsh:Neurosciences. Biological psychiatry. Neuropsychiatry, Function (biology), choanoflagellate, 030304 developmental biology, Neuroscience
Abstract

Pioneering bioinformatic analysis using sequence data revealed that teneurins evolved from bacterial tyrosine-aspartate (YD)-repeat protein precursors. Here, we discuss how structures of the C-terminal domain of teneurins, determined using X-ray crystallography and electron microscopy, support the earlier findings on the proteins’ ancestry. This chapter describes the structure of the teneurin scaffold with reference to a large family of teneurin-like proteins that are widespread in modern prokaryotes. The central scaffold of modern eukaryotic teneurins is decorated by additional domains typically found in bacteria, which are re-purposed in eukaryotes to generate highly multifunctional receptors. We discuss how alternative splicing contributed to further diversifying teneurin structure and thereby function. This chapter traces the evolution of teneurins from a structural point of view and presents the state-of-the-art of how teneurin function is encoded by its specific structural features.

Published
2019

31. Structure and flexibility of the extracellular region of the PirB receptor

Author

Vlieg, Hedwich C., Huizinga, Eric G., Janssen, Bert J. C., Sub Crystal and Structural Chemistry, Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry, and Crystal and Structural Chemistry

Subjects
0301 basic medicine, Cell signaling, Protein Conformation, Crystallography, X-Ray, Ligands, Biochemistry, Mice, 03 medical and health sciences, Neurobiology, Protein Domains, LILRB2, Extracellular, Animals, Receptors, Immunologic, Receptor, Molecular Biology, chemistry.chemical_classification, 030102 biochemistry & molecular biology, Cell Biology, Surface Plasmon Resonance, Cell biology, 030104 developmental biology, Ectodomain, chemistry, Synaptic plasticity, Glycoprotein, Intracellular, Protein Binding
Abstract

Murine paired immunoglobulin receptor B (PirB) and its human ortholog leukocyte immunoglobulin-like receptor B2 (LILRB2) are widely expressed inhibitory receptors that interact with a diverse set of extracellular ligands and exert functions ranging from down-regulation of immune responses to inhibition of neuronal growth. However, structural information that could shed light on how PirB interacts with its ligands is lacking. Here, we report crystal structures of the PirB ectodomain; the first full ectodomain structure for a LILR family member, at 3.3–4.5 Å resolution. The structures reveal that PirB's six Ig-like domains are arranged at acute angles, similar to the structures of leukocyte immunoglobulin-like receptor (LILR) and killer-cell immunoglobulin-like receptor (KIR). We observe that this regular arrangement is followed throughout the ectodomain, resulting in an extended zigzag conformation. In two out of the five structures reported here, the repeating zigzag is broken by the first domain that can adopt two alternative orientations. Quantitative binding experiments revealed a 9 μM dissociation constant for PirB–myelin-associated glycoprotein (MAG) ectodomain interactions. Taken together, these structural findings and the observed PirB—MAG interactions are compatible with a model for intercellular signaling in which the PirB extracellular domains, which point away from the cell surface, enable interaction with ligands in trans.

Published
2019

33. Inside-out or outside-in, a new factor in MAG-mediated signaling in the nervous system: An Editorial for ‘High-affinity heterotetramer formation between the large myelin-associated glycoprotein and the dynein light chain DYNLL1' on page 7

Author

Janssen, Bert J. C., Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry, Crystal and Structural Chemistry, and Sub Crystal and Structural Chemistry

Subjects
0301 basic medicine, Nervous system, Myelin-associated glycoprotein, Chemistry, Dynein, Biochemistry, Heterotetramer, Transmembrane protein, Cell biology, 03 medical and health sciences, Cellular and Molecular Neuroscience, Myelin, 030104 developmental biology, medicine.anatomical_structure, nervous system, Taverne, medicine, Axon, Function (biology)
Abstract

Our nervous system depends on protein-mediated cellular communication and connections for its formation and function. The transmembrane receptor Myelin-Associated Glycoprotein (MAG) plays an important role in the wrapping process of myelin around axons and in life-long maintenance of this important bicellular structure. MAG organizes the adhesion and the signalling between the axon and the myelin. But how does MAG do this? Better understanding of this process is required to treat MAG-function associated neurological disorders. This editorial highlights a study by Myllykoski et al. in the current issue of the Journal of Neurochemistry that describes the identification and characterization of a novel intracellular binding partner of MAG. Using cellular, biophysical and structural techniques, the authors show that the dynein light chain, DYNLL1 recognizes and interacts with only one of two splice forms of MAG, L-MAG. DYNLL1 dimerizes L-MAG at the cytosolic side and this has implications for the signalling and adhesive functions of MAG in our nervous system.

Published
2018

35. Teneurin structures are composed of ancient bacterial protein domains

Author

Sub Crystal and Structural Chemistry, Crystal and Structural Chemistry, Jackson, Verity A., Busby, Jason N., Janssen, Bert J. C., Lott, J. Shaun, Seiradake, Elena, Sub Crystal and Structural Chemistry, Crystal and Structural Chemistry, Jackson, Verity A., Busby, Jason N., Janssen, Bert J. C., Lott, J. Shaun, and Seiradake, Elena

Published
2019

38. Structural characterization of anti-CCL5 activity of the tick salivary protein evasin-4

Author

Denisov, Stepan S, Ramírez-Escudero, Mercedes, Heinzmann, Alexandra C A, Ippel, Johannes H, Dawson, Philip E, Koenen, Rory R, Hackeng, Tilman M, Janssen, Bert J C, Dijkgraaf, Ingrid, Sub Crystal and Structural Chemistry, Crystal and Structural Chemistry, Biochemie, RS: Carim - B01 Blood proteins & engineering, Sub Crystal and Structural Chemistry, and Crystal and Structural Chemistry

Subjects
0301 basic medicine, Chemokine, OLIGOMERIZATION, Peptide, Crystallography, X-Ray, Biochemistry, Protein Structure, Secondary, Protein structure, Cell Movement, immunosuppressor, Chemokine CCL5, chemistry.chemical_classification, biology, REFINEMENT, Chemistry, Ligand (biochemistry), Recombinant Proteins, 3. Good health, Cell biology, FAMILY, medicine.anatomical_structure, Protein Structure and Folding, parasite, protein&#8211, INTEGRATION, Protein Binding, nuclear magnetic resonance (NMR), CCL5, Cell Line, Protein–protein interaction, ticks, CHEMOKINE-BINDING-PROTEINS, 03 medical and health sciences, RANTES, stomatognathic system, medicine, Animals, Humans, Amino Acid Sequence, protein interaction, Salivary Proteins and Peptides, protein structure, Molecular Biology, X-ray crystallography, 030102 biochemistry & molecular biology, IDENTIFICATION, Monocyte, chemokine, Cell Biology, Protein Structure, Tertiary, N-terminus, protein–protein interaction, 030104 developmental biology, biology.protein
Abstract

Ticks, as blood-sucking parasites, have developed a complex strategy to evade and suppress host immune responses during feeding. The crucial part of this strategy is expression of a broad family of salivary proteins, called Evasins, to neutralize chemokines responsible for cell trafficking and recruitment. However, structural information about Evasins is still scarce, and little is known about the structural determinants of their binding mechanism to chemokines. Here, we studied the structurally uncharacterized Evasin-4, which neutralizes a broad range of CC-motif chemokines, including the chemokine CC-motif ligand 5 (CCL5) involved in atherogenesis. Crystal structures of Evasin-4 and E66S CCL5, an obligatory dimeric variant of CCL5, were determined to a resolution of 1.3-1.8 angstrom. The Evasin-4 crystal structure revealed an L-shaped architecture formed by an N- and C-terminal subdomain consisting of eight beta-strands and an alpha-helix that adopts a substantially different position compared with closely related Evasin-1. Further investigation into E66S CCL5-Evasin-4 complex formation with NMR spectroscopy showed that residues of the N terminus are involved in binding to CCL5. The peptide derived from the N-terminal region of Evasin-4 possessed nanomolar affinity to CCL5 and inhibited CCL5 activity in monocyte migration assays. This suggests that Evasin-4 derivatives could be used as a starting point for the development of anti-inflammatory drugs.

Published
2020

39. Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction

Author

Jackson, Verity A, Meijer, Dimphna H, Carrasquero, Maria, van Bezouwen, Laura S, Lowe, Edward D, Kleanthous, Colin, Janssen, Bert J C, Seiradake, Elena, Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry, Sub Cryo - EM, and Cryo-EM

Subjects
Membrane Glycoproteins/chemistry, Alternative Splicing/genetics, Cell Communication/physiology, Cryoelectron Microscopy, Platelet Glycoprotein GPIb-IX Complex/chemistry, Tenascin/chemistry, Crystallography, X-Ray, Protein Structure, Secondary
Abstract

Teneurins are ancient cell-cell adhesion receptors that are vital for brain development and synapse organisation. They originated in early metazoan evolution through a horizontal gene transfer event when a bacterial YD-repeat toxin fused to a eukaryotic receptor. We present X-ray crystallography and cryo-EM structures of two Teneurins, revealing a ~200 kDa extracellular super-fold in which eight sub-domains form an intricate structure centred on a spiralling YD-repeat shell. An alternatively spliced loop, which is implicated in homophilic Teneurin interaction and specificity, is exposed and thus poised for interaction. The N-terminal side of the shell is 'plugged' via a fibronectin-plug domain combination, which defines a new class of YD proteins. Unexpectedly, we find that these proteins are widespread amongst modern bacteria, suggesting early metazoan receptor evolution from a distinct class of proteins, which today includes both bacterial proteins and eukaryotic Teneurins.

Published
2018

40. Structures of Teneurin adhesion receptors reveal an ancient fold for cell-cell interaction

Author

Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry, Sub Cryo - EM, Cryo-EM, Jackson, Verity A, Meijer, Dimphna H, Carrasquero, Maria, van Bezouwen, Laura S, Lowe, Edward D, Kleanthous, Colin, Janssen, Bert J C, Seiradake, Elena, Crystal and Structural Chemistry, Sub Crystal and Structural Chemistry, Sub Cryo - EM, Cryo-EM, Jackson, Verity A, Meijer, Dimphna H, Carrasquero, Maria, van Bezouwen, Laura S, Lowe, Edward D, Kleanthous, Colin, Janssen, Bert J C, and Seiradake, Elena

Published
2018

44. A High-Resolution Crystal Structure that Reveals Molecular Details of Target Recognition by the Calcium-Dependent Lipopeptide Antibiotic Laspartomycin C

Author

Kleijn, Laurens H. J., Vlieg, Hedwich C., Wood, Thomas M., Sastre Torano, Javier, Janssen, Bert J. C., Martin, Nathaniel I., Kleijn, Laurens H. J., Vlieg, Hedwich C., Wood, Thomas M., Sastre Torano, Javier, Janssen, Bert J. C., and Martin, Nathaniel I.

Abstract

The calcium-dependent antibiotics (CDAs) are an important emerging class of antibiotics. The crystal structure of the CDA laspartomycin C in complex with calcium and the ligand geranyl-phosphate at a resolution of 1.28 Å is reported. This is the first crystal structure of a CDA bound to its bacterial target. The structure is also the first to be reported for an antibiotic that binds the essential bacterial phospholipid undecaprenyl phosphate (C55-P). These structural insights are of great value in the design of antibiotics capable of exploiting this unique bacterial target.

Published
2017

45. Nogo Receptor crystal structures with a native disulfide pattern suggest a novel mode of self-interaction

Author

Pronker, Matti F., Tas, Roderick P., Vlieg, Hedwich C., Janssen, Bert J. C., Pronker, Matti F., Tas, Roderick P., Vlieg, Hedwich C., and Janssen, Bert J. C.

Abstract

The Nogo Receptor (NgR) is a glycophosphatidylinositol-anchored cell-surface protein and is a receptor for three myelin-associated inhibitors of regeneration: myelin-associated glycoprotein, Nogo66 and oligodendrocyte myelin glyco­protein. In combination with different co-receptors, NgR mediates signalling that reduces neuronal plasticity. The available structures of the NgR ligand-binding leucine-rich repeat (LRR) domain have an artificial disulfide pattern owing to truncated C-terminal construct boundaries. NgR has previously been shown to self-associate via its LRR domain, but the structural basis of this interaction remains elusive. Here, crystal structures of the NgR LRR with a longer C-terminal segment and a native disulfide pattern are presented. An additional C-terminal loop proximal to the C-terminal LRR cap is stabilized by two newly formed disulfide bonds, but is otherwise mostly unstructured in the absence of any stabilizing interactions. NgR crystallized in six unique crystal forms, three of which share a crystal-packing interface. NgR crystal-packing interfaces from all eight unique crystal forms are compared in order to explore how NgR could self-interact on the neuronal plasma membrane.

Published
2017

46. Endometrial scratching in women with implantation failure after a first IVF/ICSI cycle; does it lead to a higher live birth rate? The SCRaTCH study : A randomized controlled trial (NTR 5342)

Author

van Hoogenhuijze, N. E., Torrance, H. L., Mol, F., Laven, Joop S E, Scheenjes, E., Traas, M.A.F., Janssen, Bert J C, Cohlen, B., Teklenburg, G., Bruin, Jacob P, van Oppenraaij, R., Maas, J. W M, Moll, Etelka, Fleischer, K., van Hooff, Marcel H, de Koning, C., Cantineau, A., Lambalk, Cornelis B., Verberg, M.F.G., Nijs, M. M., Manger, A. P., Van Rumste, M. M., Van der Voet, L F, Preys-Bosman, A., Visser, J., Brinkhuis, E.A., den Hartog, J. E., Sluijmer, A., Jansen, F. W., Hermes, W., Bandell, M. L., Pelinck, M. J., van Disseldorp, J., Wely, M., Smeenk, J., Pieterse, Q.D., Boxmeer, J.C., Groenewoud, Eva R., Eijkemans, M. J.C., Kasius, J. C., Broekmans, F. J.M., van Hoogenhuijze, N. E., Torrance, H. L., Mol, F., Laven, Joop S E, Scheenjes, E., Traas, M.A.F., Janssen, Bert J C, Cohlen, B., Teklenburg, G., Bruin, Jacob P, van Oppenraaij, R., Maas, J. W M, Moll, Etelka, Fleischer, K., van Hooff, Marcel H, de Koning, C., Cantineau, A., Lambalk, Cornelis B., Verberg, M.F.G., Nijs, M. M., Manger, A. P., Van Rumste, M. M., Van der Voet, L F, Preys-Bosman, A., Visser, J., Brinkhuis, E.A., den Hartog, J. E., Sluijmer, A., Jansen, F. W., Hermes, W., Bandell, M. L., Pelinck, M. J., van Disseldorp, J., Wely, M., Smeenk, J., Pieterse, Q.D., Boxmeer, J.C., Groenewoud, Eva R., Eijkemans, M. J.C., Kasius, J. C., and Broekmans, F. J.M.

Published
2017

47. A High-Resolution Crystal Structure that Reveals Molecular Details of Target Recognition by the Calcium-Dependent Lipopeptide Antibiotic Laspartomycin C

Author

Crystal and Structural Chemistry, Chemical Biology and Drug Discovery, Afd Chemical Biology and Drug Discovery, Sub Crystal and Structural Chemistry, Kleijn, Laurens H. J., Vlieg, Hedwich C., Wood, Thomas M., Sastre Torano, Javier, Janssen, Bert J. C., Martin, Nathaniel I., Crystal and Structural Chemistry, Chemical Biology and Drug Discovery, Afd Chemical Biology and Drug Discovery, Sub Crystal and Structural Chemistry, Kleijn, Laurens H. J., Vlieg, Hedwich C., Wood, Thomas M., Sastre Torano, Javier, Janssen, Bert J. C., and Martin, Nathaniel I.

Published
2017

49. Low pH-induced conformational change and dimerization of sortilin triggers endocytosed ligand release

Author

Sub Crystal and Structural Chemistry, Sub Biomol.Mass Spectrometry & Proteom., Afd Biomol.Mass Spect. and Proteomics, Sub Physical and Colloid Chemistry, Biomolecular Mass Spectrometry and Proteomics, Leloup, Nadia, Lössl, Philip, Meijer, Dimphna H, Brennich, Martha, Heck, Albert J R, Thies-Weesie, Dominique M E, Janssen, Bert J C, Sub Crystal and Structural Chemistry, Sub Biomol.Mass Spectrometry & Proteom., Afd Biomol.Mass Spect. and Proteomics, Sub Physical and Colloid Chemistry, Biomolecular Mass Spectrometry and Proteomics, Leloup, Nadia, Lössl, Philip, Meijer, Dimphna H, Brennich, Martha, Heck, Albert J R, Thies-Weesie, Dominique M E, and Janssen, Bert J C

Published
2017

50. Endometrial scratching in women with implantation failure after a first IVF/ICSI cycle; does it lead to a higher live birth rate? The SCRaTCH study: A randomized controlled trial (NTR 5342)

Author

UMC Utrecht, MS VPG/Gynaecologie, Fertiliteitartsen, Child Health, Infection & Immunity, Biostatistiek Onderzoek, Circulatory Health, JC onderzoeksprogramma Methodologie, JC onderzoeksprogramma Infectieziekten, Arts-assistenten DV&B, van Hoogenhuijze, N. E., Torrance, H. L., Mol, F., Laven, Joop S E, Scheenjes, E., Traas, M.A.F., Janssen, Bert J C, Cohlen, B., Teklenburg, G., Bruin, Jacob P, van Oppenraaij, R., Maas, J. W M, Moll, Etelka, Fleischer, K., van Hooff, Marcel H, de Koning, C., Cantineau, A., Lambalk, Cornelis B., Verberg, M.F.G., Nijs, M. M., Manger, A. P., Van Rumste, M. M., Van der Voet, L F, Preys-Bosman, A., Visser, J., Brinkhuis, E.A., den Hartog, J. E., Sluijmer, A., Jansen, F. W., Hermes, W., Bandell, M. L., Pelinck, M. J., van Disseldorp, J., Wely, M., Smeenk, J., Pieterse, Q.D., Boxmeer, J.C., Groenewoud, Eva R., Eijkemans, M. J.C., Kasius, J. C., Broekmans, F. J.M., UMC Utrecht, MS VPG/Gynaecologie, Fertiliteitartsen, Child Health, Infection & Immunity, Biostatistiek Onderzoek, Circulatory Health, JC onderzoeksprogramma Methodologie, JC onderzoeksprogramma Infectieziekten, Arts-assistenten DV&B, van Hoogenhuijze, N. E., Torrance, H. L., Mol, F., Laven, Joop S E, Scheenjes, E., Traas, M.A.F., Janssen, Bert J C, Cohlen, B., Teklenburg, G., Bruin, Jacob P, van Oppenraaij, R., Maas, J. W M, Moll, Etelka, Fleischer, K., van Hooff, Marcel H, de Koning, C., Cantineau, A., Lambalk, Cornelis B., Verberg, M.F.G., Nijs, M. M., Manger, A. P., Van Rumste, M. M., Van der Voet, L F, Preys-Bosman, A., Visser, J., Brinkhuis, E.A., den Hartog, J. E., Sluijmer, A., Jansen, F. W., Hermes, W., Bandell, M. L., Pelinck, M. J., van Disseldorp, J., Wely, M., Smeenk, J., Pieterse, Q.D., Boxmeer, J.C., Groenewoud, Eva R., Eijkemans, M. J.C., Kasius, J. C., and Broekmans, F. J.M.

Published
2017

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