In the budding yeast Saccharomyces cerevisiae (Baker's yeast), cell division control protein Cdc37 is required for the productive formation of Cdc28-cyclin complexes. Cdc37 may be a kinase targeting subunit of Hsp90 [].
Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This entry corresponds to the Hsp90 chaperone (heat shock protein 90) binding domain of Cdc37 []. It is found between the N-terminal Cdc37 domain (), which is predominantly involved in kinase binding, and the C-terminal domain of Cdc37 () whose function is unclear.
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 []. This entry corresponds to the Hsp90 chaperone (heat shock protein 90) binding domain of Cdc37 [].
Cdc37 is a molecular chaperone required for the activity of numerous eukaryotic protein kinases. This entry corresponds to the N-terminal kinase binding domain of these proteins []. It is found N-terminal to a Hsp90 chaperone (heat shock protein 90) binding domain (). Expression of a construct consisting of only the N-terminal domain of Saccharomyces pombe Cdc37 has been shown to result in cellular viability. This indicates that interactions with the cochaperone Hsp90 may not be essential for Cdc37 function [].
Cdc37 is a protein required for the activity of numerous eukaryotic protein kinases. This entry corresponds to the C-terminal domain whose function is unclear. It is found C-terminal to the Hsp90 chaperone (heat shock protein 90) binding domain () and the N-terminal kinase binding domain of Cdc37 () [].
