1a1o: Difference between revisions

[[Image:1a1o.gif|left|200px]]<br /><applet load="1a1o" size="350" color="white" frame="true" align="right" spinBox="true"  

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.

1A1O is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A1O OCA].  

[[Category: Bell, J I.]]

[[Category: Jones, E Y.]]

[[Category: Mcmichael, A J.]]

[[Category: Reid, S W.]]

[[Category: Smith, K J.]]

[[Category: Stuart, D I.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:39:49 2008''