2i2q
From Proteopedia
(New page: 200px<br /><applet load="2i2q" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i2q, resolution 1.720Å" /> '''Fission Yeast cofil...) |
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| - | [[Image:2i2q.gif|left|200px]]<br /><applet load="2i2q" size=" | + | [[Image:2i2q.gif|left|200px]]<br /><applet load="2i2q" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2i2q, resolution 1.720Å" /> | caption="2i2q, resolution 1.720Å" /> | ||
'''Fission Yeast cofilin'''<br /> | '''Fission Yeast cofilin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | ADF/cofilins are key regulators of actin dynamics during cellular | + | 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== | ==About this Structure== | ||
| - | 2I2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] with SO4, LDA and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2I2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe] with <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=LDA:'>LDA</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I2Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Andrianantoandro, E.]] | [[Category: Andrianantoandro, E.]] | ||
| - | [[Category: Pollard, T | + | [[Category: Pollard, T D.]] |
[[Category: EDO]] | [[Category: EDO]] | ||
[[Category: LDA]] | [[Category: LDA]] | ||
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[[Category: n-terminal serine]] | [[Category: n-terminal serine]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:48:24 2008'' |
Revision as of 15:48, 21 February 2008
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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 , and 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
Page seeded by OCA on Thu Feb 21 17:48:24 2008
