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The second metal-binding site of 70 kDa heat-shock protein is essential for ADP binding, ATP hydrolysis and ATP synthesis.

The chaperone activity of Hsp70 (70 kDa heat-shock protein) in protein folding and its conformational switch, including oligomeric and monomeric interconversion, are regulated by the hydrolysis of ATP and the ATP-ADP exchange cycle. The crystal structure of human ATPase domain shows two metal-bindin...

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Detalhes bibliográficos
Main Authors: Wu, Xueji, Yano, Mihiro, Washida, Hiroyo, Kido, Hiroshi
Formato: Artigo
Idioma:Inglês
Publicado em: 2004
Assuntos:
Acesso em linha:https://ncbi.nlm.nih.gov/pmc/articles/PMC1224023/
https://ncbi.nlm.nih.gov/pubmed/14664695
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1042/BJ20031680
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