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Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate
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 bindi...
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| Publicat a: | Proc Natl Acad Sci U S A |
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| Autors principals: | , , , , , , |
| Format: | Artigo |
| Idioma: | Inglês |
| Publicat: |
National Academy of Sciences
2016
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| Matèries: | |
| Accés en línia: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4801263/ https://ncbi.nlm.nih.gov/pubmed/26929380 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.1516167113 |
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