Effects of pseudophosphorylation mutants on the structural dynamics of smooth muscle myosin regulatory light chain
Author:
Affiliation:
1. Department of Biochemistry
2. Molecular Biology and Biophysics
3. University of Minnesota
4. Minneapolis, USA
Abstract
Phosphorylation of the regulatory light chain of smooth muscle myosin produces a unique structural balance needed for muscle activation.
Funder
American Heart Association
National Institutes of Health
Publisher
Royal Society of Chemistry (RSC)
Subject
Molecular Biology,Biotechnology
Link
http://pubs.rsc.org/en/content/articlepdf/2014/MB/C4MB00364K
Reference27 articles.
1. Refined Model of the 10S Conformation of Smooth Muscle Myosin by Cryo-electron Microscopy 3D Image Reconstruction
2. Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2
3. Kinetics of Smooth Muscle Heavy Meromyosin with One Thiophosphorylated Head
4. Modification of Interface between Regulatory and Essential Light Chains Hampers Phosphorylation-dependent Activation of Smooth Muscle Myosin
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