The functional binding site for the C-type lectin-like natural killer cell receptor Ly49A spans three domains of its major histocompatibility complex class I ligand

Journal of Experimental Medicine

Volumn 193, Issue 2, 2001, Pages 147-157

  Matsumoto, Naoki ^a   Mitsuki, Motoaki ^a   Tajima, Kyoko ^a   Yokoyama, Wayne M ^b   Yamamoto, Kazuo ^a  

^a UNIVERSITY OF TOKYO   (Japan)

^b WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

2 Microglobulin; Cytotoxicity; H 2 antigens; Inhibitory receptor; Mutation

Indexed keywords

BETA 2 MICROGLOBULIN; CD8 ANTIGEN; LECTIN RECEPTOR; LIGAND; LYSINE; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1;

ANIMAL CELL; ARTICLE; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CYTOTOXICITY; HYDROGEN BOND; MOLECULAR RECOGNITION; MOUSE; NATURAL KILLER CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RECEPTOR BINDING; TARGET CELL;

ANIMALS; ANTIGENS, CD8; ANTIGENS, LY; BASE SEQUENCE; BETA 2-MICROGLOBULIN; BINDING SITES; CARRIER PROTEINS; CELL LINE; DNA PRIMERS; H-2 ANTIGENS; HUMANS; KILLER CELLS, NATURAL; LECTINS; LECTINS, C-TYPE; LIGANDS; MACROMOLECULAR SUBSTANCES; MEMBRANE PROTEINS; MICE; MICE, INBRED C57BL; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, IMMUNOLOGIC; TRANSFECTION;

EID: 0035862324     PISSN: 00221007     EISSN: None     Source Type: Journal    
DOI: 10.1084/jem.193.2.147     Document Type: Article

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