Post-Translational Modification as an Allosteric Switch in Hsp90: How Dual Phosphorylation Locks Chaperone Complexes
Giorgio Bonollo1, Benedetto Roncati1, Luca Torielli1
1Department of Chemistry, University of Pavia, Via Taramelli 12, 27100, Pavia, Italy.
Abstract:
Multimicrosecond MD simulations reveal that dual phosphorylation at Ser226/Ser255 of Hsp90β acts as a molecular clamp, rigidifying the overall structure, propagating allosteric coordination changes to distal domains, and stabilizing cochaperone-client interfaces. These findings provide an atomistic mechanism by which post-translational modifications can stabilize Hsp90 interaction states that are compatible with epichaperome formation, with implications for disease biology and therapeutic targeting.
Related Concept Videos
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Covalently Linked Protein Regulators
These groups modify specific amino acids in a protein.
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Cooperative Allosteric Transitions
Molecular Chaperones and Protein Folding
The...


