Analysis of the human cofilin 1 structure reveals conformational changes required for actin binding.

@article{Klejnot2013AnalysisOT,
  title={Analysis of the human cofilin 1 structure reveals conformational changes required for actin binding.},
  author={Marta Klejnot and Mads Gabrielsen and Jenifer M. Cameron and Andrzej Mleczak and Sandeep K Talapatra and Frank Kozielski and Andrew Pannifer and Michael F Olson},
  journal={Acta crystallographica. Section D, Biological crystallography},
  year={2013},
  volume={69 Pt 9},
  pages={
          1780-8
        }
}
The actin cytoskeleton is the chassis that gives a cell its shape and structure, and supplies the power for numerous dynamic processes including motility, endocytosis, intracellular transport and division. To perform these activities, the cytoskeleton undergoes constant remodelling and reorganization. One of the major actin-remodelling families are the cofilin proteins, made up of cofilin 1, cofilin 2 and actin-depolymerizing factor (ADF), which sever aged ADP-associated actin filaments to… CONTINUE READING
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