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Grp94, the endoplasmic reticulum Hsp90, has a similar solution conformation to cytosolic Hsp90 in the absence of nucleotide

The molecular chaperone, Hsp90, is an essential eukaryotic protein that assists in the maturation and activation of client proteins. Hsp90 function depends upon the binding and hydrolysis of ATP, which causes large conformational rearrangements in the chaperone. Hsp90 is highly conserved from bacter...

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Библиографические подробности
Главные авторы: Krukenberg, Kristin A, Böttcher, Ulrike M K, Southworth, Daniel R, Agard, David A
Формат: Artigo
Язык:Inglês
Опубликовано: Wiley Subscription Services, Inc., A Wiley Company 2009
Предметы:
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC2777357/
https://ncbi.nlm.nih.gov/pubmed/19554567
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1002/pro.191
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