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1a1n
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(New page: 200px<br /> <applet load="1a1n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a1n, resolution 2.0Å" /> '''MHC CLASS I MOLECULE...)
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Revision as of 11:42, 8 November 2007
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MHC CLASS I MOLECULE B*3501 COMPLEXED WITH PEPTIDE VPLRPMTY FROM THE NEF PROTEIN (75-82) OF HIV1
Overview
The crystal structure of the human major histocompatibility complex class, I B allele HLA B*3501 complexed with the 8-mer peptide epitope HIV1 Nef, 75-82 (VPLRPMTY) has been determined at 2.0 angstrom resolution., Comparison with the crystal structure of the closely related allele HLA, B*5301 reveals the structural basis for the tyrosine specificity of the, B*3501 F pocket. The structure also reveals a novel conformation of the, 8-mer peptide within the binding groove. The positions of the peptide N, and C termini are nonstandard, but the classic pattern of hydrogen bonding, to nonpolymorphic MHC class I residues is maintained, at the N terminus by, addition of a water molecule, and at the C terminus by a substantial shift, in the alpha 2 helix.
About this Structure
1A1N is a Protein complex structure of sequences from Homo sapiens and Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
An altered position of the alpha 2 helix of MHC class I is revealed by the crystal structure of HLA-B*3501., Smith KJ, Reid SW, Stuart DI, McMichael AJ, Jones EY, Bell JI, Immunity. 1996 Mar;4(3):203-13. PMID:8624811
Page seeded by OCA on Thu Nov 8 13:48:44 2007
