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The ATPase cycle of Hsp90 drives a molecular ‘clamp’ via transient dimerization of the N-terminal domains

How the ATPase activity of Heat shock protein 90 (Hsp90) is coupled to client protein activation remains obscure. Using truncation and missense mutants of Hsp90, we analysed the structural implications of its ATPase cycle. C-terminal truncation mutants lacking inherent dimerization displayed reduced...

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Detalhes bibliográficos
Main Authors: Prodromou, Chrisostomos, Panaretou, Barry, Chohan, Shahzad, Siligardi, Giuliano, O’Brien, Ronan, Ladbury, John E., Roe, S.Mark, Piper, Peter W., Pearl, Laurence H.
Formato: Artigo
Idioma:Inglês
Publicado em: Oxford University Press 2000
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC302038/
https://ncbi.nlm.nih.gov/pubmed/10944121
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/19.16.4383
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