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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Vydáno v:Proc Natl Acad Sci U S A
Hlavní autoři: Sung, Nuri, Lee, Jungsoon, Kim, Ji-Hyun, Chang, Changsoo, Joachimiak, Andrzej, Lee, Sukyeong, Tsai, Francis T. F.
Médium: Artigo
Jazyk:Inglês
Vydáno: National Academy of Sciences 2016
Témata:
Biological Sciences
On-line přístup: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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