Client binding of Cdc37 is regulated intramolecularly and intermolecularly
Kazuya Terasawa1, Fumika Shinozaki, Michiko Minami
1Department of Biophysics and Biochemistry, Graduate School of Science, The University of Tokyo.
Abstract:
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.
More Related Videos
10:33Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors
Published on: October 26, 2015
10:17Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
Published on: January 14, 2020
Related Concept Videos
Cooperative Binding of Transcription Regulators
Assembly of Signaling Complexes
Interaction domains in cell signaling
Interaction domains recognize exposed features of their binding partners containing post-translationally modified sequences,...
Ligand Binding and Linkage
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Cooperative Allosteric Transitions
Cis-regulatory Sequences
