The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC

Cell

Volumn 70, Issue 6, 1992, Pages 1035-1048

  Madden, Dean R ^a   Gorga, Joan C ^a   Strominger, Jack L ^a   Wiley, Don C ^a,b  

^a HARVARD UNIVERSITY   (United States)

^b UNIVERSITY OF CAMBRIDGE   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

HLA B27 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MEMBRANE ANTIGEN;

ARTICLE; BIOLOGICAL MODEL; CRYSTALLIZATION; CYTOTOXIC T LYMPHOCYTE; DISEASE ASSOCIATION; INFORMATION PROCESSING; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY;

AMINO ACID SEQUENCE; ARGININE; HLA-B27 ANTIGEN; HUMAN; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; STRUCTURE-ACTIVITY RELATIONSHIP; SUPPORT, NON-U.S. GOV'T; SUPPORT, U.S. GOV'T, P.H.S.; X-RAY DIFFRACTION;

EID: 0026794581     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/0092-8674(92)90252-8     Document Type: Article

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