Structural and Functional Analysis of the Middle Segment of Hsp90: Implications for ATP Hydrolysis and Client Protein and Cochaperone Interactions

Activation of client proteins by the Hsp90 molecular chaperone is dependent on binding and hydrolysis of ATP, which drives a molecular clamp via transient dimerization of the N-terminal domains. The crystal structure of the middle segment of yeast Hsp90 reveals considerable evolutionary divergence f...

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Veröffentlicht in:	Molecular cell 2003-03, Vol.11 (3), p.647-658
Hauptverfasser:	Meyer, Philippe, Prodromou, Chrisostomos, Hu, Bin, Vaughan, Cara, Roe, S. Mark, Panaretou, Barry, Piper, Peter W., Pearl, Laurence H.
Format:	Artikel
Sprache:	eng
Schlagworte:	Adenosine Triphosphatases - metabolism Adenosine Triphosphate - metabolism Amino Acid Sequence Binding Sites Cell Division Crystallography, X-Ray Dimerization DNA Gyrase - metabolism Dose-Response Relationship, Drug Escherichia coli Proteins - metabolism Fungal Proteins - chemistry HSP90 Heat-Shock Proteins - chemistry HSP90 Heat-Shock Proteins - metabolism Hydrolysis Models, Molecular Molecular Sequence Data Mutation MutL Proteins Oncogene Protein pp60(v-src) - metabolism Phenotype Protein Binding Protein Conformation Protein Structure, Tertiary Structure-Activity Relationship Temperature
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