2i2q

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[[Image:2i2q.gif|left|200px]]
[[Image:2i2q.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 2i2q |SIZE=350|CAPTION= <scene name='initialview01'>2i2q</scene>, resolution 1.720&Aring;
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The line below this paragraph, containing "STRUCTURE_2i2q", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= cof1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 Schizosaccharomyces pombe])
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|DOMAIN=
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{{STRUCTURE_2i2q| PDB=2i2q | SCENE= }}
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|RELATEDENTRY=[[1cof|1COF]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2i2q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i2q OCA], [http://www.ebi.ac.uk/pdbsum/2i2q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2i2q RCSB]</span>
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'''Fission Yeast cofilin'''
'''Fission Yeast cofilin'''
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[[Category: Andrianantoandro, E.]]
[[Category: Andrianantoandro, E.]]
[[Category: Pollard, T D.]]
[[Category: Pollard, T D.]]
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[[Category: n-terminal serine]]
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[[Category: N-terminal serine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 07:00:06 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:38:50 2008''
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Revision as of 04:00, 4 May 2008

Image:2i2q.gif

Template:STRUCTURE 2i2q

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. 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 Sun May 4 07:00:06 2008

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