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455 results on '"Kuriyan J"'

1. Structural analysis of autoinhibition in the Ras-specific exchange factor RasGRP1

Author

Roose, Jeroen, Iwig, JS, Vercoulen, Y, Das, R, Barros, T, Limnander, A, Che, Y, Pelton, JG, Wemmer, DE, Roose, JP, and Kuriyan, J

Abstract

RasGRP1 and SOS are Ras-specific nucleotide exchange factors that have distinct roles in lymphocyte development. RasGRP1 is important in some cancers and autoimmune diseases but, in contrast to SOS, its regulatory mechanisms are poorly understood. Activati

Published
2013

18. B-Raf:14-3-3 complex

Author

Kondo, Y., primary, Ognjenovic, J., additional, Banerjee, S., additional, Karandur, D., additional, Merk, A., additional, Kulhanek, K., additional, Wong, K., additional, Roose, J.P., additional, Subramaniam, S., additional, and Kuriyan, J., additional

Published
2019
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22. Molecular mechanism of activation-triggered subunit exchange in Ca2+/calmodulin-dependent protein kinase II

Author

Bhattacharyya, M, Stratton, MM, Going, CC, McSpadden, ED, Huang, Y, Susa, AC, Elleman, A, Cao, YM, Pappireddi, N, Burkhardt, P, Gee, CL, Barros, T, Schulman, H, Williams, ER, and Kuriyan, J

Subjects
enzymes and coenzymes (carbohydrates), musculoskeletal, neural, and ocular physiology, cardiovascular system, environment and public health
Abstract

© Bhattacharyya et al. Activation triggers the exchange of subunits in Ca2+/calmodulin-dependent protein kinase II (CaMKII), an oligomeric enzyme that is critical for learning, memory, and cardiac function. The mechanism by which subunit exchange occurs remains elusive. We show that the human CaMKII holoenzyme exists in dodecameric and tetradecameric forms, and that the calmodulin (CaM)-binding element of CaMKII can bind to the hub of the holoenzyme and destabilize it to release dimers. The structures of CaMKII from two distantly diverged organisms suggest that the CaM-binding element of activated CaMKII acts as a wedge by docking at intersubunit interfaces in the hub. This converts the hub into a spiral form that can release or gain CaMKII dimers. Our data reveal a three-way competition for the CaM-binding element, whereby phosphorylation biases it towards the hub interface, away from the kinase domain and calmodulin, thus unlocking the ability of activated CaMKII holoenzymes to exchange dimers with unactivated ones.

Published
2016
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30. Emerging concepts in the regulation of the EGF receptor and other receptor tyrosine kinases

Author

Endres, NF, Barros, T, Cantor, AJ, and Kuriyan, J

Subjects
Protein Structure, EGF Family of Proteins, allostery, Epidermal Growth Factor, receptor tyrosine kinases, Protein Conformation, Cell Membrane, Receptor Protein-Tyrosine Kinases, Biological Sciences, Ligands, Medical and Health Sciences, Enzyme Activation, ErbB Receptors, Chemical Sciences, Humans, Protein Multimerization, epidermal growth factor receptor, Tertiary, signal transduction, Receptor, Developmental Biology
Abstract

© 2014 Elsevier Ltd. The activation of receptor tyrosine kinases in response to extracellular signals is a principal component of metazoan signaling. Structural analysis of the extracellular and intracellular domains of these receptors has shed substantial light on the mechanisms underlying their activation. A remaining challenge is to understand how these domains operate together in the context of the full-length receptors. With a focus on the epidermal growth factor (EGF) receptor, this review highlights recent advances towards this goal. Although receptor tyrosine kinases are divergent in terms of the details of how they operate, these studies reveal common mechanisms that ensure activation in the proper context. Understanding these mechanisms provides insights into the vulnerabilities of these receptors to disease-causing mutations.

Published
2014
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32. A structural at~las of kinases inhibited by clinically approved drugs

Author

Wang, Q, Zorn, JA, and Kuriyan, J

Abstract

© 2014 Elsevier Inc. All rights reserved. The aberrant activation of protein kinases is associated with many human diseases, most notably cancer. Due to this link between kinase deregulation and disease progression, kinases are one of the most targeted protein families for small-molecule inhibition. Within the last 15 years, the U.S. Food and Drug Administration has approved over 20 small-molecule inhibitors of protein kinases for use in the clinic. These inhibitors target the kinase active site and represent the successful hurdling by medicinal chemists of the formidable challenge posed by the high similarity among the active sites of the approximately 500 human kinases. We review the conserved structural features of kinases that are important for inhibitor binding as well as for catalysis. Many clinically approved drugs elicit selectivity by exploiting subtle variation within the kinase active site. We highlight some of the crystallographic studies on the kinase-inhibitor complexes that have provided valuable guidance for the development of these drugs as well as for future drug design efforts.

Published
2014
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48. C2 can do it, too

Author

Sondermann, H. and Kuriyan, J.

Subjects
Protein kinases -- Research, Threonine -- Research, Serine -- Research, Biological sciences
Abstract

A study conducted reports that the C2 domain of the serine/threonine protein kinase Cdelta is a phosphotyrosine binding domain. Details of the crystal structure of this C2 domain bound to a peptide containing phosphotyrosine are presented.

Published
2005

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