2i2q
From Proteopedia
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Fission Yeast cofilin
Overview
ADF/cofilins are key regulators of actin dynamics during cellular, motility, yet their precise role and mechanism of action are shrouded in, ambiguity. Direct observation of actin filaments by evanescent wave, microscopy showed that cofilins from fission yeast and human do not, increase the rate that pointed ends of actin filaments shorten beyond the, rate for ADP-actin subunits, but both cofilins inhibit elongation and, subunit dissociation at barbed ends. Direct observation also showed that, cofilins from fission yeast, Acanthamoeba, and human sever actin filaments, optimally at low-cofilin binding densities well below their K(d)s, but not, at high binding densities. High concentrations of cofilin nucleate actin, assembly. Thus, the action of cofilins in cells will depend on the local, concentration of active cofilins: low concentrations favor severing, whereas high concentrations favor nucleation. These results establish a, clear paradigm for actin turnover by cofilin in cells.
About this Structure
2I2Q is a Single protein structure of sequence from Schizosaccharomyces pombe with SO4, LDA and EDO as ligands. Full crystallographic information is available from OCA.
Reference
Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin., Andrianantoandro E, Pollard TD, Mol Cell. 2006 Oct 6;24(1):13-23. PMID:17018289
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