1a1o

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[[Image:1a1o.gif|left|200px]]
[[Image:1a1o.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1a1o", creates the "Structure Box" on the page.
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|GENE= T7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1a1o| PDB=1a1o | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a1o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a1o OCA], [http://www.ebi.ac.uk/pdbsum/1a1o PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a1o RCSB]</span>
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'''MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE LS6 (KPIVQYDNF) FROM THE MALARIA PARASITE P. FALCIPARUM'''
'''MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE LS6 (KPIVQYDNF) FROM THE MALARIA PARASITE P. FALCIPARUM'''
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[[Category: Smith, K J.]]
[[Category: Smith, K J.]]
[[Category: Stuart, D I.]]
[[Category: Stuart, D I.]]
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[[Category: complex (antigen/peptide)]]
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[[Category: Hla]]
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[[Category: hla]]
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[[Category: Hla-b53]]
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[[Category: hla-b53]]
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[[Category: Major histocompatibility antigen]]
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[[Category: major histocompatibility antigen]]
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[[Category: Malaria]]
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[[Category: malaria]]
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[[Category: Mhc]]
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[[Category: mhc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 09:40:23 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:31:10 2008''
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Revision as of 06:40, 2 May 2008

Image:1a1o.gif

Template:STRUCTURE 1a1o

MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE LS6 (KPIVQYDNF) FROM THE MALARIA PARASITE P. FALCIPARUM


Overview

The structure of the human MHC class I molecule HLA-B53 complexed to two nonameric peptide epitopes (from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography at 2.3 angstrom resolution. The structures reveal the architecture of a Pro-specific B pocket common to many HLA-B alleles. Relative to other alleles, the B53 peptide-binding groove is widened by a significant (up to 1.25 angstrom) shift in the position of the alpha 1 helix. Within this groove, bound water molecules, acting in concert with the side chains of polymorphic residues, provide the functional malleability of the MHC, which enables the high affinity/low specificity binding of multiple peptide epitopes.

About this Structure

1A1O is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53., Smith KJ, Reid SW, Harlos K, McMichael AJ, Stuart DI, Bell JI, Jones EY, Immunity. 1996 Mar;4(3):215-28. PMID:8624812 Page seeded by OCA on Fri May 2 09:40:23 2008

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