1jtp
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
1JTP is a Protein complex structure of sequences from Camelus dromedarius and Meleagris gallopavo 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
Page seeded by OCA on Sun Nov 18 09:34:15 2007
Categories: Camelus dromedarius | Lysozyme | Meleagris gallopavo | Protein complex | Decanniere, K. | Desmyter, A. | Maes, D. | Muyldermans, S. | Transue, T.R. | Wyns, L. | FMT | NA | Binding | Heavy chain antibody | Immunoglobulin | Interface | Vhh
