Structures of GRP94-Nucleotide Complexes Reveal Mechanistic Differences between the hsp90 Chaperones

Molecular Cell

Volumn 28, Issue 1, 2007, Pages 41-56

  Dollins, D Eric ^a,b   Warren, Joshua J ^b   Immormino, Robert M ^a,b   Gewirth, Daniel T ^a  

^a HAUPTMAN WOODWARD MEDICAL RESEARCH INSTITUTE   (United States)

^b DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

PROTEINS

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; CHAPERONE; GLUCOSE REGULATED PROTEIN 94; HEAT SHOCK PROTEIN 90;

AMINO TERMINAL SEQUENCE; ARTICLE; COMPLEX FORMATION; CRYSTAL STRUCTURE; DIMERIZATION; ENZYME ACTIVITY; HYDROLYSIS; PROTEIN BINDING; PROTEIN CONFORMATION;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; ADENYLYL IMIDODIPHOSPHATE; ANIMALS; CRYSTALLOGRAPHY, X-RAY; DIMERIZATION; DOGS; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY;

MAMMALIA;

EID: 34948893963     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2007.08.024     Document Type: Article

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