Ontology highlight
ABSTRACT:
SUBMITTER: Liu Y
PROVIDER: S-EPMC3123929 | biostudies-literature | 2011 Jun
REPOSITORIES: biostudies-literature
Liu Yanxin Y Hsin Jen J Kim HyeongJun H Selvin Paul R PR Schulten Klaus K
Biophysical journal 20110601 12
The molecular motor protein myosin VI moves toward the minus-end of actin filaments with a step size of 30-36 nm. Such large step size either drastically limits the degree of complex formation between dimer subunits to leave enough length for the lever arms, or requires an extension of the lever arms' crystallographically observed structure. Recent experimental work proposed that myosin VI dimerization triggers the unfolding of the protein's proximal tail domain which could drive the needed leve ...[more]