1a1o
From Proteopedia
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MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE LS6 (KPIVQYDNF) FROM THE MALARIA PARASITE P. FALCIPARUM
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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.
Disease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]
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 Mon Nov 12 15:54:22 2007
