1a1o

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(New page: 200px<br /> <applet load="1a1o" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a1o, resolution 2.3&Aring;" /> '''MHC CLASS I MOLECULE...)
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Revision as of 11:42, 8 November 2007

Image:1a1o.gif

1a1o, resolution 2.3Å

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MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE LS6 (KPIVQYDNF) FROM THE MALARIA PARASITE P. FALCIPARUM

Overview

The structure of the human MHC class I molecule HLA-B53 complexed to two, nonameric peptide epitopes (from the malaria parasite P. falciparum and, the HIV2 gag protein) has been determined by X-ray crystallography at 2.3, angstrom resolution. The structures reveal the architecture of a, Pro-specific B pocket common to many HLA-B alleles. Relative to other, alleles, the B53 peptide-binding groove is widened by a significant (up to, 1.25 angstrom) shift in the position of the alpha 1 helix. Within this, groove, bound water molecules, acting in concert with the side chains of, polymorphic residues, provide the functional malleability of the MHC, which enables the high affinity/low specificity binding of multiple, peptide epitopes.

About this Structure

1A1O is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53., Smith KJ, Reid SW, Harlos K, McMichael AJ, Stuart DI, Bell JI, Jones EY, Immunity. 1996 Mar;4(3):215-28. PMID:8624812

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