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2 results on '"Sebastian Fenn"'

1. Crystal structure of an anti-Ang2 CrossFab demonstrates complete structural and functional integrity of the variable domain.

Author

Sebastian Fenn, Christian B Schiller, Julia J Griese, Harald Duerr, Sabine Imhof-Jung, Christian Gassner, Joerg Moelleken, Joerg Thomas Regula, Wolfgang Schaefer, Markus Thomas, Christian Klein, Karl-Peter Hopfner, and Hubert Kettenberger

Subjects
Medicine, Science
Abstract

Bispecific antibodies are considered as a promising class of future biotherapeutic molecules. They comprise binding specificities for two different antigens, which may provide additive or synergistic modes of action. There is a wide variety of design alternatives for such bispecific antibodies, including the "CrossMab" format. CrossMabs contain a domain crossover in one of the antigen-binding (Fab) parts, together with the "knobs-and-holes" approach, to enforce the correct assembly of four different polypeptide chains into an IgG-like bispecific antibody. We determined the crystal structure of a hAng-2-binding Fab in its crossed and uncrossed form and show that CH1-CL-domain crossover does not induce significant perturbations of the structure and has no detectable influence on target binding.

Published
2013
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2. Crystal structure of an anti-Ang2 CrossFab demonstrates complete structural and functional integrity of the variable domain

Author

Christian Gassner, Christian Klein, Joerg Thomas Regula, Julia J. Griese, Sabine Imhof-Jung, Wolfgang Schaefer, Joerg Moelleken, Karl-Peter Hopfner, Hubert Kettenberger, Christian B. Schiller, Sebastian Fenn, Harald Duerr, and Markus Thomas

Subjects
Models, Molecular, Macromolecular Assemblies, Crossover, Immunoglobulin Variable Region, lcsh:Medicine, Bioinformatics, Crystallography, X-Ray, Biochemistry, Protein structure, Structural Biology, Static electricity, Antibodies, Bispecific, Drug Discovery, Macromolecular Structure Analysis, Biomacromolecule-Ligand Interactions, lcsh:Science, Peptide sequence, Strukturbiologi, Multidisciplinary, Protein Stability, Immunoglobulin Fab Fragments, Immunochemistry, Temperature, Research Article, Biotechnology, Protein Structure, Molecular Sequence Data, Static Electricity, Immunology, Biophysics, Biomedical Engineering, Immunoglobulins, Bioengineering, Protein Chemistry, Angiopoietin-2, Structure-Activity Relationship, Antigen, Structure–activity relationship, Humans, Amino Acid Sequence, Biology, lcsh:R, Proteins, Computational Biology, Protein Structure, Tertiary, HEK293 Cells, Structural biology, lcsh:Q
Abstract

Bispecific antibodies are considered as a promising class of future biotherapeutic molecules. They comprise binding specificities for two different antigens, which may provide additive or synergistic modes of action. There is a wide variety of design alternatives for such bispecific antibodies, including the "CrossMab" format. CrossMabs contain a domain crossover in one of the antigen-binding (Fab) parts, together with the "knobs-and-holes" approach, to enforce the correct assembly of four different polypeptide chains into an IgG-like bispecific antibody. We determined the crystal structure of a hAng-2-binding Fab in its crossed and uncrossed form and show that CH1-CL-domain crossover does not induce significant perturbations of the structure and has no detectable influence on target binding.

Published
2013

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