The three-dimensional structure of an H-2Ld-peptide complex explains the unique interaction of Ld with beta-2 microglobulin and peptide

Proceedings of the National Academy of Sciences of the United States of America

Volumn 94, Issue 13, 1997, Pages 6880-6885

  Balendiran, Ganesaratnam K ^a   Solheim, Joyce C ^b   Young, Aideen C M ^c   Hansen, Ted H ^b   Nathenson, Stanley G ^c   Sacchettini, James C ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BETA 2 MICROGLOBULIN; H2 ANTIGEN; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

ANIMAL CELL; ANTIGEN EXPRESSION; ANTIGEN PRESENTATION; ARTICLE; CELL SURFACE; COMPLEX FORMATION; CONTROLLED STUDY; HYDROGEN BOND; HYDROPHOBICITY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE;

ANIMALS; BETA 2-MICROGLOBULIN; CRYSTALLIZATION; H-2 ANTIGENS; ISOANTIGENS; MICE; PROTEIN CONFORMATION;

ANIMALIA;

EID: 0030917013     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.13.6880     Document Type: Article

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