1e28: Difference between revisions

Revision as of 00:01, 1 July 2008

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File:1e28.png

Template:STRUCTURE 1e28

NONSTANDARD PEPTIDE BINDING OF HLA-B5101 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM2(TAFTIPSI)NONSTANDARD PEPTIDE BINDING OF HLA-B5101 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM2(TAFTIPSI)

Template:ABSTRACT PUBMED 10975842

About this StructureAbout this Structure

1E28 is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

ReferenceReference

Nonstandard peptide binding revealed by crystal structures of HLA-B*5101 complexed with HIV immunodominant epitopes., Maenaka K, Maenaka T, Tomiyama H, Takiguchi M, Stuart DI, Jones EY, J Immunol. 2000 Sep 15;165(6):3260-7. PMID:10975842

Page seeded by OCA on Tue Jul 1 00:01:27 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 {{STRUCTURE_1e28|  PDB=1e28  |  SCENE=  }}
-'''NONSTANDARD PEPTIDE BINDING OF HLA-B*5101 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM2(TAFTIPSI)'''
+===NONSTANDARD PEPTIDE BINDING OF HLA-B*5101 COMPLEXED WITH HIV IMMUNODOMINANT EPITOPE KM2(TAFTIPSI)===
-==Overview==
+<!--
-The crystal structures of the human MHC class I allele HLA-B*5101 in complex with 8-mer, TAFTIPSI, and 9-mer, LPPVVAKEI, immunodominant peptide epitopes from HIV-1 have been determined by x-ray crystallography. In both complexes, the hydrogen-bonding network in the N-terminal anchor (P1) pocket is rearranged as a result of the replacement of the standard tyrosine with histidine at position 171. This results in a nonstandard positioning of the peptide N terminus, which is recognized by B*5101-restricted T cell clones. Unexpectedly, the P5 peptide residues appear to act as anchors, drawing the peptides unusually deeply into the peptide-binding groove of B51. The unique characteristics of P1 and P5 are likely to be responsible for the zig-zag conformation of the 9-mer peptide and the slow assembly of B*5101. A comparison of the surface characteristics in the alpha1-helix C-terminal region for B51 and other MHC class I alleles highlights mainly electrostatic differences that may be important in determining the specificity of human killer cell Ig-like receptor binding.
+The line below this paragraph, {{ABSTRACT_PUBMED_10975842}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10975842 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10975842}}
 ==About this Structure==
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 [[Category: Hla b51]]
 [[Category: Mhc class i]]
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