Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate. [electronic resource]
Producer: 20160811Description: 2952-7 p. digitalISSN:- 1091-6490
- Adenosine Triphosphate -- chemistry
- Allosteric Regulation
- Allosteric Site
- Amino Acid Motifs
- Amino Acid Sequence
- Amino Acid Substitution
- Animals
- Binding Sites
- Computer Simulation
- Crystallography, X-Ray
- HSP70 Heat-Shock Proteins -- metabolism
- HSP90 Heat-Shock Proteins -- chemistry
- Humans
- Mitochondria -- metabolism
- Models, Molecular
- Molecular Sequence Data
- Protein Binding
- Protein Conformation
- Protein Folding
- Rabbits
- Recombinant Fusion Proteins -- chemistry
- Sequence Homology, Amino Acid
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Publication Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
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