1t5x: Difference between revisions

Revision as of 23:55, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1t5x.png

Template:STRUCTURE 1t5x

HLA-DR1 in complex with a synthetic peptide (AAYSDQATPLLLSPR) and the superantigen SEC3-3B2HLA-DR1 in complex with a synthetic peptide (AAYSDQATPLLLSPR) and the superantigen SEC3-3B2

Template:ABSTRACT PUBMED 15489166

About this StructureAbout this Structure

1T5X is a Protein complex structure of sequences from Homo sapiens and Staphylococcus aureus. Full crystallographic information is available from OCA.

ReferenceReference

A polymorphic pocket at the P10 position contributes to peptide binding specificity in class II MHC proteins., Zavala-Ruiz Z, Strug I, Anderson MW, Gorski J, Stern LJ, Chem Biol. 2004 Oct;11(10):1395-402. PMID:15489166

Page seeded by OCA on Sun Jul 27 23:55:31 2008

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-'''HLA-DR1 in complex with a synthetic peptide (AAYSDQATPLLLSPR) and the superantigen SEC3-3B2'''
+===HLA-DR1 in complex with a synthetic peptide (AAYSDQATPLLLSPR) and the superantigen SEC3-3B2===
-==Overview==
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-Peptides bind to class II major histocompatibility complex (MHC) proteins in an extended conformation. Pockets in the peptide binding site spaced to accommodate peptide side chains at the P1, P4, P6, and P9 positions have been previously characterized and help to explain the obtained peptide binding specificity. However, two peptides differing only at P10 have significantly different binding affinities for HLA-DR1. The structure of HLA-DR1 in complex with the tighter binding peptide shows that the peptide binds in the usual polyproline type II conformation, but with the P10 residue accommodated in a shallow pocket at the end of the binding groove. HLA-DR1 variants with polymorphic residues at these positions were produced and found to exhibit different side chain specificity at the P10 position. These results define a new specificity position in HLA-DR proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_15489166}}, adds the Publication Abstract to the page
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