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
Date Published2001 Oct 26
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

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.

Alternate JournalJ. Mol. Biol.
PubMed ID11676532