Structural effects of cofilin on longitudinal contacts in F-actin.

@article{Bobkov2002StructuralEO,
  title={Structural effects of cofilin on longitudinal contacts in F-actin.},
  author={Andrey A. Bobkov and Andras Muhlrad and Kaveh Kokabi and Sergey Vorobiev and Steven C. Almo and Emil Reisler},
  journal={Journal of molecular biology},
  year={2002},
  volume={323 4},
  pages={739-50}
}
Structural effects of yeast cofilin on skeletal muscle and yeast actin were examined in solution. Cofilin binding to native actin was non-cooperative and saturated at a 1:1 molar ratio, with K(d)<or=0.05 microM for both CaATP-G-actin and F-actin. Cofilin binding enhanced the fluorescence of dansyl ethylenediamine (DED) attached to Gln41 on the DNase I binding loop of skeletal muscle F-actin and decreased the fluorescence of AEDANS at Cys41 on yeast Q41C/C374S mutant F-actin. However, cofilin… CONTINUE READING