A5024995322- Heat shock proteins research
- Enzyme Structure and Function
- Protein Structure and Dynamics
- Cellular transport and secretion
- Erythrocyte Function and Pathophysiology
- ATP Synthase and ATPases Research
- Endoplasmic Reticulum Stress and Disease
- Toxin Mechanisms and Immunotoxins
- Advanced Thermodynamic Systems and Engines
- Biochemical and Molecular Research
Institut de Biologie Structurale
2021-2024
Centre National de la Recherche Scientifique
2022-2024
CEA Grenoble
2022-2024
Commissariat à l'Énergie Atomique et aux Énergies Alternatives
2022-2024
Université Grenoble Alpes
2022-2024
Abstract HSP90 are abundant molecular chaperones, assisting the folding of several hundred client proteins, including substrates involved in tumor growth or neurodegenerative diseases. A complex set large ATP-driven structural changes occurs during functional cycle. However, existence such rearrangements apo has remained unclear. Here, we identify a metastable excited state isolated human HSP90α ATP binding domain. We use solution NMR and mutagenesis to characterize structures both ground...
Abstract HSP90 are abundant molecular chaperones, assisting the folding of several hundred client proteins, including substrates involved in tumor growth or neurodegenerative diseases. A complex set large ATP-driven structural changes occurs during functional cycle. However, existence such rearrangements apo has remained unclear. Here, we identified a metastable excited state isolated ATP binding domain. We used solution NMR and mutagenesis to characterize structures both ground states....