1a1m: Difference between revisions
No edit summary |
No edit summary |
||
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= GAG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= GAG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a1m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a1m OCA], [http://www.ebi.ac.uk/pdbsum/1a1m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a1m RCSB]</span> | |||
}} | }} | ||
| Line 14: | Line 17: | ||
==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. | ||
==About this Structure== | ==About this Structure== | ||
1A1M is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/ | 1A1M is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_2 Human immunodeficiency virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A1M OCA]. | ||
==Reference== | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/8624812 8624812] | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8624812 8624812] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Human immunodeficiency virus | [[Category: Human immunodeficiency virus 2]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Bell, J I.]] | [[Category: Bell, J I.]] | ||
| Line 40: | Line 40: | ||
[[Category: mhc]] | [[Category: mhc]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:31:08 2008'' | ||