Client Binding of Cdc37 Is Regulated Intramolecularly and Intermolecularly
Recently we showed that the glycine-rich loop in the N-terminal portion of protein kinases and the client-binding site of Cdc37 are both necessary for interaction between Cdc37 and protein kinases. We demonstrate here that the N-terminal portion of Cdc37, distinct from its client-binding site, interacts with the C-terminal portion of Raf-1. This interaction might expose the client-binding site of Cdc37. In addition, we provide evidence indicating that Cdc37 is monomeric in its physiological state, and that it becomes a dimer only when it is complexed with both Hsp90 and protein kinases.
- Bioscience, biotechnology, and biochemistry
Bioscience, biotechnology, and biochemistry 70(6), 1542-1546, 2006-06-23
Japan Society for Bioscience, Biotechnology, and Agrochemistry