1jto
From Proteopedia
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Degenerate interfaces in antigen-antibody complexes
Overview
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.
About this Structure
1JTO is a Protein complex structure of sequences from Camelus dromedarius and Gallus gallus. Active as Lysozyme, with EC number 3.2.1.17 Full crystallographic information is available from OCA.
Reference
Degenerate interfaces in antigen-antibody complexes., Decanniere K, Transue TR, Desmyter A, Maes D, Muyldermans S, Wyns L, J Mol Biol. 2001 Oct 26;313(3):473-8. PMID:11676532
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