Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure...
Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate
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Publisher
United States: National Academy of Sciences
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Language
English
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United States: National Academy of Sciences
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Contents
Heat-shock protein of 90 kDa (Hsp90) is an essential molecular chaperone that adopts different 3D structures associated with distinct nucleotide states: a wide-open, V-shaped dimer in the apo state and a twisted, N-terminally closed dimer with ATP. Although the N domain is known to mediate ATP binding, how Hsp90 senses the bound nucleotide and faci...
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Full title
Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate
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TN_cdi_proquest_journals_1779194125
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_journals_1779194125
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ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1516167113
