Structure of unliganded GRP94, the endoplasmic reticulum Hsp90: Basis for nucleotide-induced conformational change

Journal of Biological Chemistry

Volumn 280, Issue 34, 2005, Pages 30438-30447

  Dollins, D Eric ^a   Immormino, Robert M ^a   Gewirth, Daniel T ^a  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINETRIPHOSPHATE; CONFORMATIONS; CRYSTALLINE MATERIALS; ENZYME INHIBITION; ENZYMES;

ENDOPLASMIC RETICULUM; LIGANDS; NUCLEOTIDES;

CELL MEMBRANES;

ADENINE NUCLEOTIDE; CHAPERONE; HEAT SHOCK PROTEIN 90; PROTEIN GRP94; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; LIGAND BINDING; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SEQUENCE; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; ELECTRONS; ENDOPLASMIC RETICULUM; ESCHERICHIA COLI; HSP70 HEAT-SHOCK PROTEINS; HSP90 HEAT-SHOCK PROTEINS; HYDROGEN BONDING; LIGANDS; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID;

EID: 24044518180     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M503761200     Document Type: Article

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