1e28

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[[Image:1e28.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e28 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e28 OCA], [http://www.ebi.ac.uk/pdbsum/1e28 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e28 RCSB]</span>
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'''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)'''
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[[Category: Takiguchi, M.]]
[[Category: Takiguchi, M.]]
[[Category: Tomiyama, H.]]
[[Category: Tomiyama, H.]]
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[[Category: histocompatibility complex]]
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[[Category: Histocompatibility complex]]
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[[Category: hiv]]
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[[Category: Hiv]]
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[[Category: hla b51]]
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[[Category: Hla b51]]
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[[Category: mhc class i]]
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[[Category: Mhc class i]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:34:02 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:53:27 2008''
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Revision as of 11:34, 2 May 2008

Template:STRUCTURE 1e28

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.

About 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.

Reference

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 Fri May 2 14:34:02 2008

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