1eo8
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(New page: 200px<br /> <applet load="1eo8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1eo8, resolution 2.8Å" /> '''INFLUENZA VIRUS HEMA...)
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Revision as of 07:22, 18 November 2007
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INFLUENZA VIRUS HEMAGGLUTININ COMPLEXED WITH A NEUTRALIZING ANTIBODY
Overview
The structure of a complex between the hemagglutinin of influenza virus, and the Fab of a neutralizing antibody was determined by X-ray, crystallography at 2.8 A resolution. This antibody and another which has, only 56% sequence identity bind to the same epitope with very similar, affinities and in the same orientation. One third of the interactions is, conserved in the two complexes; a significant proportion of the, interactions that differ are established by residues of the H3, complementarity-determining regions (CDR) which adopt distinct, conformations in the two antibodies. This demonstrates that there is a, definite flexibility in the selection of antibodies that bind to a given, epitope, despite the high affinity of their complexes. This flexibility, allows the humoral immune response to be redundant, a feature that may be, useful in achieving longer lasting protection against evolving viral, pathogens.
About this Structure
1EO8 is a Protein complex structure of sequences from Influenza a virus and Mus musculus with NAG as ligand. Full crystallographic information is available from OCA.
Reference
Structural evidence for recognition of a single epitope by two distinct antibodies., Fleury D, Daniels RS, Skehel JJ, Knossow M, Bizebard T, Proteins. 2000 Sep 1;40(4):572-8. PMID:10899782
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