Degenerate interfaces in antigen-antibody complexes.

TitleDegenerate interfaces in antigen-antibody complexes.
Publication TypeJournal Article
Year of Publication2001
AuthorsDecanniere, K., T. R. Transue, A. Desmyter, D. Maes, S. Muyldermans, and L. Wyns
JournalJ Mol Biol
Volume313
Issue3
Pagination473-8
Date Published2001 Oct 26
ISSN0022-2836
KeywordsAnimals, Antigen-Antibody Complex, Binding Sites, Antibody, Camels, Chickens, Crystallography, X-Ray, Egg White, Female, Immunoglobulin Variable Region, Models, Molecular, Muramidase, Peptide Fragments, Protein Conformation
Abstract

In most of the work dealing with the analysis of protein-protein interfaces, a single X-ray structure is available or selected, and implicitly it is assumed that this structure corresponds to the optimal complex for this pair of proteins. However, we have found a degenerate interface in a high-affinity antibody-antigen complex: the two independent complexes of the camel variable domain antibody fragment cAb-Lys3 and its antigen hen egg white lysozyme present in the asymmetric unit of our crystals show a difference in relative orientation between antibody and antigen, leading to important differences at the protein-protein interface. A third cAb-Lys3-hen lysozyme complex in a different crystal form adopts yet another relative orientation. Our results show that protein-protein interface characteristics can vary significantly between different specimens of the same high-affinity antibody-protein antigen complex. Consideration should be given to this type of observation when trying to establish general protein-protein interface characteristics.

DOI10.1006/jmbi.2001.5075
Alternate JournalJ. Mol. Biol.
PubMed ID11676532