1jtt

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spinqualitylabelsall models 1jtt, resolution 2.1Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

1JTT is a Protein complex structure of sequences from Camelus dromedarius and Gallus gallus with NA and FMT as ligands. 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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