Literature summary for 3.6.4.10 extracted from

McLaughlin, S.H.; Sobott, F.; Yao, Z.P.; Zhang, W.; Nielsen, P.R.; Grossmann, J.G.; Laue, E.D.; Robinson, C.V.; Jackson, S.E.
The co-chaperone p23 arrests the Hsp90 ATPase cycle to trap client proteins (2006), J. Mol. Biol., 356, 746-758.

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Inhibitors

Inhibitors	Comment	Organism	Structure
p23 protein	cochaperone, interacts with Hsp90 in both the absence and presence of nucleotide, with a higher affinity in presence of the ATP analogue 5'-adenylyl-beta,gamma-imidodiphosphate. Mixed inhibition, one p23 binds to each subunit of the Hsp90 dimer. Complex formation between Hsp90 and p23 increases the apparent affinity of Hsp90 for 5'-adenylyl-beta,gamma-imidodiphosphate and completely inhibits the ATPase activity	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	isoform Hsp90	-

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Release 2023.1 (January 2023)