Structure of a phage display-derived variant of human growth hormone complexed to two copies of the extracellular domain of its receptor: Evidence for strong structural coupling between receptor binding sites

Journal of Molecular Biology

Volumn 316, Issue 2, 2002, Pages 277-289

  Schiffer, Celia ^a   Ultsch, Mark ^a   Walsh, Scott ^b   Somers, William ^a   De Vos, Abraham M ^a   Kossiakoff, Anthony ^a,b,c  

^a GENENTECH INC   (United States)

^b UNIVERSITY OF CHICAGO   (United States)

^c UNIVERSITY OF CHICAGO   (United States)

Author keywords

Cytokine hormone receptor complex; Molecular plasticity; Phage display; Protein protein interactions; Receptor homodimerization

Indexed keywords

ASPARTIC ACID; GROWTH HORMONE; GROWTH HORMONE RECEPTOR; MUTANT PROTEIN; RECEPTOR SUBTYPE; TRYPTOPHAN;

ARTICLE; BINDING AFFINITY; BINDING ASSAY; BINDING SITE; CARBOXY TERMINAL SEQUENCE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; GENE MUTATION; HORMONE RECEPTOR INTERACTION; HUMAN; HYDROGEN BOND; HYDROPHOBICITY; PHAGE DISPLAY; PLASTICITY; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN TERTIARY STRUCTURE; PROTEIN VARIANT;

EID: 0036289017     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.5348     Document Type: Article

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