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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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Bibliografski detalji
Glavni autori: Chadli, Ahmed, Bouhouche, Ilham, Sullivan, William, Stensgard, Bridget, McMahon, Nancy, Catelli, Maria G., Toft, David O.
Format: Artigo
Jezik:Inglês
Izdano: The National Academy of Sciences 2000
Teme:
Online pristup:https://ncbi.nlm.nih.gov/pmc/articles/PMC18797/
https://ncbi.nlm.nih.gov/pubmed/11050175
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