Journal ArticleDOI
Crystal structures of two mutant neuraminidase-antibody complexes with amino acid substitutions in the interface.
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TLDR
The results provide a basis for understanding some of the potential structural effects of somatic hypermutation on antigen-antibody binding in those cases where the mutation in the antibody occurs at antigen-contacting residues, and demonstrate the importance of structural context in evaluating the effect of amino acid substitutions on protein structure and function.About:
This article is published in Journal of Molecular Biology.The article was published on 1992-09-05. It has received 84 citations till now. The article focuses on the topics: Neuraminidase & Mutant.read more
Citations
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Journal ArticleDOI
Effects of amino acid sequence changes on antibody-antigen interactions.
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Anatomy of the antibody molecule
TL;DR: The structures of the various regions of an antibody molecule are analysed and correlated with biological function and potential applications are detailed.
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Interactions of protein antigens with antibodies.
David R. Davies,Gerson H. Cohen +1 more
TL;DR: There are now several crystal structures of antibody Fab fragments complexed to their protein antigens, with good shape complementarity between the interacting surfaces and reasonable juxtapositions of polar residues so as to permit hydrogen-bond formation.
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Influenza virus neuraminidase: structure, antibodies, and inhibitors.
TL;DR: The determination of the 3‐dimensional structure of the influenza virus neuraminidase in 1983 has served as a platform for understanding interactions between antibodies and protein antigens, for investigating antigenic variation in influenza viruses, and for devising new inhibitors of the enzyme.
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Antibody-antigen interactions
Ian A. Wilson,Robyn L. Stanfield +1 more
TL;DR: The structures of several free and bound Fabs show that induced-fit mechanisms best describe the antibody-antigen recognition process and affects the prediction, engineering and design of antibody combining sites.
References
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The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
Pamela J. Bjorkman,Pamela J. Bjorkman,Pamela J. Bjorkman,Mark A. Saper,Boudjéma Samraoui,W. S. Bennett,W. S. Bennett,Jack L. Strominger,Don C. Wiley +8 more
TL;DR: Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens.
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Deciphering the message in protein sequences: tolerance to amino acid substitutions
TL;DR: Comparison of different sequences with similar messages can reveal key features of the code and improve understanding of how a protein folds and how it performs its function.
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A graphics model building and refinement system for macromolecules
TL;DR: A model building and refinement system is described for use with a Vector General 3400 display that has been used to assist in difference Fourier map interpretation at medium and high resolution, and to build a protein molecule into a multiple isomorphous replacement phased electron density map.
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Traitement statistique des erreurs dans la determination des structures cristallines
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Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution
TL;DR: The 2.8 A resolution three-dimensional structure of a complex between an antigen (lysozyme) and the Fab fragment from a monoclonal antibody against lysozyme has been determined and refined by x-ray crystallographic techniques.