[HTML][HTML] Hsp90· Cdc37 complexes with protein kinases form cooperatively with multiple distinct interaction sites
JM Eckl, MJ Scherr, L Freiburger, MA Daake… - Journal of Biological …, 2015 - ASBMB
Protein kinases are the most prominent group of heat shock protein 90 (Hsp90) clients and
are recruited to the molecular chaperone by the kinase-specific cochaperone cell division
cycle 37 (Cdc37). The interaction between Hsp90 and nematode Cdc37 is mediated by
binding of the Hsp90 middle domain to an N-terminal region of Caenorhabditis elegans
Cdc37 (CeCdc37). Here we map the binding site by NMR spectroscopy and define amino
acids relevant for the interaction between CeCdc37 and the middle domain of Hsp90. Apart …
are recruited to the molecular chaperone by the kinase-specific cochaperone cell division
cycle 37 (Cdc37). The interaction between Hsp90 and nematode Cdc37 is mediated by
binding of the Hsp90 middle domain to an N-terminal region of Caenorhabditis elegans
Cdc37 (CeCdc37). Here we map the binding site by NMR spectroscopy and define amino
acids relevant for the interaction between CeCdc37 and the middle domain of Hsp90. Apart …