View source for 1qpv

==YEAST COFILIN==
<StructureSection load='1qpv' size='340' side='right' caption='[[1qpv]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1qpv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QPV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QPV FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cfy|1cfy]], [[1cof|1cof]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qpv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qpv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qpv RCSB], [http://www.ebi.ac.uk/pdbsum/1qpv PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/COFI_YEAST COFI_YEAST]] Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. Binding to F-actin is regulated by tropomyosin. It is the major component of intranuclear and cytoplasmic actin rods. Required for accumulation of actin at the cell division site via depolymerizing actin at the cell ends. In association with myosin II has a role in the assembly of the contractile ring via severing actin filaments. Involved in the maintenance of the contractile ring once formed. In association with profilin and capping protein, has a role in the mitotic reorganization of the actin cytoskeleton. In effect, yeast cofilin increases the rate of actin polymerization by making new ends available for actin subunit addition. Such a protein complex is important for the polarized growth of yeast cells.<ref>PMID:10231390</ref> <ref>PMID:11747431</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qp/1qpv_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cofilin, a ubiquitous 15,000 M(r) protein, plays a central role in regulating cytoskeletal dynamics. Cofilin binds to actin monomers and filaments, and has a pH-dependent actin severing activity. The structure will allow for a detailed analysis of cofilin function.

Structure determination of yeast cofilin.,Fedorov AA, Lappalainen P, Fedorov EV, Drubin DG, Almo SC Nat Struct Biol. 1997 May;4(5):366-9. PMID:9145106<ref>PMID:9145106</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Saccharomyces cerevisiae]]
[[Category: Almo, S C]]
[[Category: Drubin, D G]]
[[Category: Fedorov, A A]]
[[Category: Fedorov, E V]]
[[Category: Lappalainen, P]]
[[Category: Actin-binding protein]]
[[Category: Cofilin fold]]
[[Category: Three layers:alpha/mixed beta/alpha]]