InterPro domain: IPR038189

Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. The C-terminal segment of Cdc37 is entirely helical in structure, consisting of a large 6-helix bundle at the N-terminal end, connected to a small 3-helix bundle via a long single helix. The Hsp90 N-terminal nucleotide binding domain binds to the large helical domain of Cdc37 [ 1 ]. This entry corresponds to the Hsp90 chaperone (heat shock protein 90) binding domain of Cdc37 [ 2 ].

1. The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37). Cell 116, 87-98
2. Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90. FEBS J. 272, 4129-40