2i2q
From Proteopedia
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|PDB= 2i2q |SIZE=350|CAPTION= <scene name='initialview01'>2i2q</scene>, resolution 1.720Å | |PDB= 2i2q |SIZE=350|CAPTION= <scene name='initialview01'>2i2q</scene>, resolution 1.720Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |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> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= cof1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 Schizosaccharomyces pombe]) | |GENE= cof1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 Schizosaccharomyces pombe]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1cof|1COF]] | ||
| + | |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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[[Category: Andrianantoandro, E.]] | [[Category: Andrianantoandro, E.]] | ||
[[Category: Pollard, T D.]] | [[Category: Pollard, T D.]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: LDA]] | ||
| - | [[Category: SO4]] | ||
[[Category: n-terminal serine]] | [[Category: n-terminal serine]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:38:50 2008'' |
Revision as of 00:38, 31 March 2008
| |||||||
| , resolution 1.720Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Gene: | cof1 (Schizosaccharomyces pombe) | ||||||
| Related: | 1COF
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Mon Mar 31 03:38:50 2008
