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Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53.

Abstract:

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 th...

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Publication status:
Published

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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Experimental Medicine Division,
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Biology
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Journal:
Immunity
Volume:
4
Issue:
3
Pages:
215-228
Publication date:
1996-03-05
DOI:
EISSN:
1097-4180
ISSN:
1074-7613
URN:
uuid:b193fcc8-7422-411d-a1bf-75f20473c050
Source identifiers:
26830
Local pid:
pubs:26830

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