Structural basis for the dynamic chaperoning of disordered clients by Hsp90

Molecular chaperone heat shock protein 90 (Hsp90) is a ubiquitous regulator that fine-tunes and remodels diverse client proteins, exerting profound effects on normal biology and diseases. Unraveling the mechanistic details of Hsp90’s function requires atomic-level insights into its client interactio...

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Veröffentlicht in:	Nature structural & molecular biology 2024-10, Vol.31 (10), p.1482-1491
Hauptverfasser:	Qu, Xiaozhan, Zhao, Shuo, Wan, Chanjuan, Zhu, Lei, Ji, Tuo, Rossi, Paolo, Wang, Junfeng, Kalodimos, Charalampos G., Wang, Chao, Xu, Weiya, Huang, Chengdong
Format:	Artikel
Sprache:	eng
Schlagworte:	631/45/470/1981 631/535/878/1263 Adenosine triphosphate Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism ATP Binding Sites Biochemistry Biological effects Biological Microscopy Biomedical and Life Sciences Clients Heat shock proteins HSP90 Heat-Shock Proteins - chemistry HSP90 Heat-Shock Proteins - metabolism Hsp90 protein Humans Hydrophobic and Hydrophilic Interactions Hydrophobicity Life Sciences Magnetic resonance spectroscopy Membrane Biology Models, Molecular NMR NMR spectroscopy Nuclear capture Nuclear magnetic resonance Nuclear Magnetic Resonance, Biomolecular Protein Binding Protein Conformation Protein Structure Proteins Spectroscopy Spectrum analysis Structure-function relationships
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