Prediction and dissection of widely-varying association rate constants of actin-binding proteins.

ABSTRACT: Actin is an abundant protein that constitutes a main component of the eukaryotic cytoskeleton. Its polymerization and depolymerization are regulated by a variety of actin-binding proteins. Their functions range from nucleation of actin polymerization to sequestering G-actin in 1∶1 complexes. The kinetics of forming these complexes, with rate constants varying at least three orders of magnitude, is critical to the distinct regulatory functions. Previously we have developed a transient-complex theory for computing protein association mechanisms and association rate constants. The transient complex refers to an intermediate in which the two associating proteins have near-native separation and relative orientation but have yet to form short-range specific interactions of the native complex. Th

SUBMITTER: Pang X 

PROVIDER: S-EPMC3464195 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature