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Updated: May 14, 2026

Probing Myosin Ensemble Mechanics in Actin Filament Bundles Using Optical Tweezers
Published on: May 4, 2022
Structural insight into the UNC-45-myosin complex
Filip Fratev1, Svava Osk Jónsdóttir, Ilza Pajeva
1Micar 21 Ltd., 1470 Sofia, Bulgaria. fratev@clbme.bas.bg
Abstract:
The UNC-45 chaperone protein interacts with and affects the folding, stability, and the ATPase activity of myosins. It plays a critical role in the cardiomyopathy development and in the breast cancer tumor growth. Here we propose the first structural model of the UNC-45-myosin complex using various in silico methods. Initially, the human UNC-45B binding epitope was identified and the protein was docked to the cardiac myosin (MYH7) motor domain. The final UNC45B-MYH7 structure was obtained by performing of total 630 ns molecular dynamics simulations. The results indicate a complex formation, which is mainly stabilized by electrostatic interactions. Remarkably, the contact surface area is similar to that of the myosin-actin complex. A significant interspecies difference in the myosin binding epitope is observed. Our results reveal the structural basis of MYH7 exons 15-16 hypertrophic cardiomyopathy mutations and provide directions for drug targeting.
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