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- W2288960304 abstract "Significance Mitochondrial heat-shock protein of 90 kDa (Hsp90) (TRAP1) promotes cell survival and is essential for neoplastic growth. Exploiting human TRAP1 for drug development requires detailed structural and mechanistic understanding. Whereas TRAP1 adopts different conformations associated with distinct nucleotide states, how the TRAP1 dimer senses the bound nucleotide and signals this information to the neighboring subunit remains unknown. We show that unliganded TRAP1 forms a previously unobserved coiled-coil dimer and is found in an autoinhibited state. ATP binding in cis displaces the ATP lid that signals the nucleotide status to the trans subunit. Our findings suggest that human TRAP1 is a ligand-activated molecular chaperone, which couples ATP binding to local changes in structure facilitating dimer closure needed for protein folding." @default.
- W2288960304 created "2016-06-24" @default.
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- W2288960304 date "2016-02-29" @default.
- W2288960304 modified "2023-10-14" @default.
- W2288960304 title "Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate" @default.
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- W2288960304 doi "https://doi.org/10.1073/pnas.1516167113" @default.
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