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Importance of cycle timing for the function of the molecular chaperone Hsp90

Hsp90 couples ATP hydrolysis to large conformational changes essential for activation of client proteins. The structural transitions involve dimerization of the N-terminal domains and formation of ‘closed states’ involving the N-terminal and middle domains. Here, we used Hsp90 mutants that modulate...

Täydet tiedot

Tallennettuna:
Bibliografiset tiedot
Julkaisussa:Nat Struct Mol Biol
Päätekijät: Zierer, Bettina K, Rübbelke, Martin, Tippel, Franziska, Madl, Tobias, Schopf, Florian H, Rutz, Daniel A, Richter, Klaus, Sattler, Michael, Buchner, Johannes
Aineistotyyppi: Artigo
Kieli:Inglês
Julkaistu: 2016
Aiheet:
Linkit:https://ncbi.nlm.nih.gov/pmc/articles/PMC6248305/
https://ncbi.nlm.nih.gov/pubmed/27723736
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1038/nsmb.3305
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