Degenerate interfaces in antigen-antibody complexes.

K Decanniere; T R Transue; A Desmyter; D Maes; S Muyldermans; L Wyns

doi:10.1006/jmbi.2001.5075

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Degenerate interfaces in antigen-antibody complexes.

K Decanniere·T R Transue·A Desmyter·D Maes·S Muyldermans·L Wyns

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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.

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K Decanniere, T R Transue, A Desmyter, D Maes, S Muyldermans, L Wyns. 2001-10-26. Degenerate interfaces in antigen-antibody complexes.. https://doi.org/10.1006/jmbi.2001.5075

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