Dimerization and N-terminal domain proximity underlie the function of the molecular chaperone heat shock protein 90

Heat shock protein (hsp)90 functions in a complex chaperoning pathway where its activity is modulated by ATP and by interaction with several co-chaperones. One co-chaperone, p23, binds selectively to the ATP-bound state of hsp90. However, the isolated ATP-binding domain of hsp90 does not bind p23. I...

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Vydáno v:	Proc Natl Acad Sci U S A
Hlavní autoři:	Chadli, Ahmed, Bouhouche, Ilham, Sullivan, William, Stensgard, Bridget, McMahon, Nancy, Catelli, Maria G., Toft, David O.
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	National Academy of Sciences 2000
Témata:	Biological Sciences
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC18797/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/11050175/ https://ncbi.nlm.nih.govhttps://doi.org/10.1073/pnas.220430297
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