Molecular basis for barbed end uncapping by CARMIL homology domain 3 of mouse CARMIL-1.

@article{Zwolak2010MolecularBF,
  title={Molecular basis for barbed end uncapping by CARMIL homology domain 3 of mouse CARMIL-1.},
  author={Adam Zwolak and Takehito Uruno and Grzegorz Piszczek and John A Hammer and Nico Tjandra},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 37},
  pages={
          29014-26
        }
}
Capping protein (CP) is a ubiquitously expressed, 62-kDa heterodimer that binds the barbed end of the actin filament with approximately 0.1 nm affinity to prevent further monomer addition. CARMIL is a multidomain protein, present from protozoa to mammals, that binds CP and is important for normal actin dynamics in vivo. The CARMIL CP binding site resides in its CAH3 domain (CARMIL homology domain 3) located at or near the protein's C terminus. CAH3 binds CP with approximately 1 nm affinity… CONTINUE READING
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