Conserved Conformational Changes in the ATPase Cycle of Human Hsp90

The dimeric molecular chaperone Hsp90 is required for the activation and stabilization of hundreds of substrate proteins, many of which participate in signal transduction pathways. The activation process depends on the hydrolysis of ATP by Hsp90. Hsp90 consists of a C-terminal dimerization domain, a...

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Veröffentlicht in:	The Journal of biological chemistry 2008-06, Vol.283 (26), p.17757-17765
Hauptverfasser:	Richter, Klaus, Soroka, Joanna, Skalniak, Lukasz, Leskovar, Adriane, Hessling, Martin, Reinstein, Jochen, Buchner, Johannes
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - chemistry Adenosine Triphosphate - chemistry Chromatography Cytosol - metabolism Dimerization Dose-Response Relationship, Drug Fungal Proteins - chemistry Gene Deletion HSP90 Heat-Shock Proteins - chemistry Humans Hydrolysis Kinetics Protein Conformation Protein Structure, Tertiary
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