The complex dance of the molecular chaperone Hsp90.
Hsp90 chaperone function requires traversal of a nucleotide-dependent conformational cycle, but the slow and variable rate of Hsp90-mediated ATP hydrolysis is difficult to envision as a determinant of conformational change. A recent study solves this dilemma by showing that Hsp90 samples multiple conformational states in the absence of nucleotides, which serve to influence, but not direct, the cycle. The conformational program of Hsp90 is conserved from bacteria to humans, although the population dynamics are species specific.
Urologic Oncology Branch, Center for Cancer Research, National Cancer Institute, NIH, Bethesda, MD 20892, USA. len@helix.nih.gov
Len
L
Neckers
Mehdi
M
Mollapour
Shinji
S
Tsutsumi
D000818:Animals; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D006801:Humans; D008962:Models, Theoretical; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D011487:Protein Conformation
D018841:HSP90 Heat-Shock Proteins; D018832:Molecular Chaperones