1a1m: Difference between revisions

Revision as of 15:47, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1a1m.png

Template:STRUCTURE 1a1m

MHC CLASS I MOLECULE B5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2MHC CLASS I MOLECULE B5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2

Template:ABSTRACT PUBMED 8624812

About this StructureAbout this Structure

1A1M is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 2. 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

Page seeded by OCA on Mon Jun 30 15:47:47 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1a1m.gif|left|200px]]
+{{Seed}}
+[[Image:1a1m.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1a1m|  PDB=1a1m  |  SCENE=  }}
-'''MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2'''
+===MHC CLASS I MOLECULE B*5301 COMPLEXED WITH PEPTIDE TPYDINQML FROM GAG PROTEIN OF HIV2===
-==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 line below this paragraph, {{ABSTRACT_PUBMED_8624812}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8624812 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8624812}}
 ==About this Structure==
@@ Line 35: / Line 39: @@
 [[Category: Major histocompatibility antigen]]
 [[Category: Mhc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 09:40:18 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 15:47:47 2008''