Client Binding of Cdc37 Is Regulated Intramolecularly and Intermolecularly
Copyright policy )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.
- Tokyo Gakugei University Japan
- University of Tokyo Japan
Proto-Oncogene Proteins c-raf, COS Cells, Chlorocebus aethiops, Animals, Cell Cycle Proteins, HSP90 Heat-Shock Proteins, Dimerization, Protein Binding
Proto-Oncogene Proteins c-raf, COS Cells, Chlorocebus aethiops, Animals, Cell Cycle Proteins, HSP90 Heat-Shock Proteins, Dimerization, Protein Binding
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