1a1m: Difference between revisions
New page: left|200px<br /> <applet load="1a1m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a1m, resolution 2.3Å" /> '''MHC CLASS I MOLECULE... |
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==Overview== | ==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. | 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:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]], Hypoproteinemia, hypercatabolic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=109700 109700]], Spondyloarthropathy, susceptibility to, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=142830 142830]] | |||
==About this Structure== | ==About this Structure== | ||
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[[Category: mhc]] | [[Category: mhc]] | ||
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Revision as of 16:47, 12 November 2007
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MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2
OverviewOverview
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.
DiseaseDisease
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 StructureAbout this Structure
1A1M is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
ReferenceReference
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
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