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HSP90AA1 — TPT1

Text-mined interactions from Literome

Weikl et al., J Mol Biol 1999 : These results imply that the binding site for Hsp90 is contained in the folded domain of p23 and that for efficient interaction of p23 with non-native proteins both the folded domain and the C-terminal unstructured region are required
Young et al., EMBO J 2000 : The co-chaperone p23 greatly stimulates Hsp90 substrate release with ATP, but not with the non-hydrolysable nucleotides ATPgammaS or AMP-PNP
Zhang et al., Cell Stress Chaperones 2010 : p23 binds to the ATP bound form of Hsp90 and stabilizes the Hsp90-client protein complex by slowing down ATP turnover
Blacklock et al., PloS one 2013 : According to our results, p23 mediated changes in the Hsp90 interactions may provide `` molecular brakes '' that could slow down an efficient transmission of the inter-domain allosteric signals, consistent with the functional role of p23 in partially inhibiting the ATPase cycle