1fyt: Difference between revisions

Revision as of 04:08, 1 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:1fyt.png

Template:STRUCTURE 1fyt

CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELL RECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS II MOLECULE, HLA-DR1CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELL RECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS II MOLECULE, HLA-DR1

Template:ABSTRACT PUBMED 11060013

About this StructureAbout this Structure

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

ReferenceReference

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

Page seeded by OCA on Tue Jul 1 04:08:42 2008

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OCA

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 {{STRUCTURE_1fyt|  PDB=1fyt  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF A COMPLEX OF A HUMAN ALPHA/BETA-T CELL RECEPTOR, INFLUENZA HA ANTIGEN PEPTIDE, AND MHC CLASS II MOLECULE, HLA-DR1'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_11060013}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11060013 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11060013}}
 ==About this Structure==
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 [[Category: Immunoglobulin fold]]
 [[Category: Protein-protein complex]]
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