Download MendeleyDegenerate interfaces in antigen-antibody complexes.
Decanniere, K., Transue, T.R., Desmyter, A., Maes, D., Muyldermans, S., Wyns, L.(2001) J Mol Biol 313: 473-478
- PubMed: 11676532
- DOI: https://doi.org/10.1006/jmbi.2001.5075
- Primary Citation of Related Structures:
1JTO, 1JTP, 1JTT - PubMed 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.
Organizational Affiliation:
Vrije Universiteit Brussel Dienst Ultrastructuur, Vlaams Instituut voor Biotechnologie, Paardenstraat 65, B-1640 St.-Genesius Rode, Belgium. [email protected]
