NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol

ChemBioChem

Volumn 4, Issue 9, 2003, Pages 870-877

  Dehner, Alexander ^a   Furrer, Julien ^a   Richter, Klaus ^a   Schuster, Ioana ^a   Buchner, Johannes ^a   Kessler, Horst ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

ATPase; Chaperone proteins; Inhibitors; NMR spectroscopy; Protein structure; Protein ligand interactions

Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATASE; ADENYLYLIMIDODIPHOSPHATE; CHAPERONE; GELDANAMYCIN; HEAT SHOCK PROTEIN 90; LIGAND; RADICICOL;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; LIGAND BINDING; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTON NUCLEAR MAGNETIC RESONANCE; X RAY CRYSTALLOGRAPHY;

ADENYLYL IMIDODIPHOSPHATE; AMINO ACID SEQUENCE; BENZOQUINONES; BINDING SITES; ESCHERICHIA COLI; HSP90 HEAT-SHOCK PROTEINS; LACTAMS, MACROCYCLIC; LACTONES; MACROLIDES; MAGNETIC RESONANCE SPECTROSCOPY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, SECONDARY; QUINONES;

EID: 0141683523     PISSN: 14394227     EISSN: None     Source Type: Journal    
DOI: 10.1002/cbic.200300658     Document Type: Article

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