Kinesin-5 allosteric inhibitors uncouple the dynamics of nucleotide, microtubule, and neck-linker binding sites.

Abstract excerpt

Kinesin motor domains couple cycles of ATP hydrolysis to cycles of microtubule binding and conformational changes that result in directional force and movement on microtubules. The general principles of this mechanochemical coupling have been established; however, fundamental atomistic details of the underlying allosteric mechanisms remain unknown. This lack of knowledge hampers the development of new inhibitors...

Topics

Share this publication in a Topic to start or enrich a Post.

• Share to Adenosine Diphosphate
• Share to Adenosine Triphosphate
• Share to Allosteric Regulation