1cfq

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Revision as of 14:51, 8 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1cfq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cfq, resolution 2.8Å" /> '''ANTI-P24 (HIV-1) FAB...)
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File:1cfq.gif


1cfq, resolution 2.8Å

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ANTI-P24 (HIV-1) FAB FRAGMENT CB41

OverviewOverview

The X-ray crystal structures of an anti-p24 (HIV-1) monoclonal antibody, Fab fragment alone and in complexes with the epitope peptide GATPQDLNTnL, (n = norleucine), an epitope-homologous peptide GATPEDLNQKLAGN, as well as, two unrelated peptides GLYEWGGARITNTD and efslkGpllqwrsG (D-peptide), are, presented to a maximum resolution of 2.6 A. The latter three peptides were, identified from screening synthetic combinatorial peptide libraries., Although all peptides bind to the same antigen combining site, the, nonhomologous peptides adopt different binding conformations and also form, their critical contacts with different antibody residues. Only small, readjustments are observed within the framework of the Fab fragment upon, binding.

About this StructureAbout this Structure

1CFQ is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity., Keitel T, Kramer A, Wessner H, Scholz C, Schneider-Mergener J, Hohne W, Cell. 1997 Dec 12;91(6):811-20. PMID:9413990

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