1fyt

From Proteopedia

Revision as of 14:52, 12 November 2007

CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELL RECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS II MOLECULE, HLA-DR1

Overview

An alphabeta T-cell receptor (alphabetaTCR)/hemagglutinin (HA), peptide/human leukocyte antigen (HLA)-DR1 complex was stabilized by, flexibly linking the HA peptide with the human HA1.7 alphabetaTCR, to, increase the local concentration of the interacting proteins once the, peptide has been loaded onto the major histocompatibility complex (MHC), molecule. The structure of the complex, determined by X-ray, crystallography, has a binding mode similar to that of the human B7, alphabetaTCR on a pMHCI molecule. Twelve of the 15 MHC residues contacted, are at the same positions observed earlier in class I MHC/peptide/TCR, complexes. One contact, to an MHC loop outside the peptide-binding site, is conserved and specific to pMHCII complexes. TCR gene usage in the, response to HA/HLA-DR appears to conserve charged interactions between, three lysines of the peptide and acidic residues on the TCR.

About this Structure

1FYT is a Protein complex structure of sequences from Homo sapiens and Influenza a virus (a/hong kong(h3n2)) with NAG as ligand. Full crystallographic information is available from OCA.

Reference

Structure of a covalently stabilized complex of a human alphabeta T-cell receptor, influenza HA peptide and MHC class II molecule, HLA-DR1., Hennecke J, Carfi A, Wiley DC, EMBO J. 2000 Nov 1;19(21):5611-24. PMID:11060013

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