1nr0

<table><tr><td colspan='2'>[[1nr0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Caeel Caeel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NR0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1NR0 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">UNC-78 OR C04F6.4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6239 CAEEL])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1nr0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nr0 OCA], [http://pdbe.org/1nr0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nr0 RCSB], [http://www.ebi.ac.uk/pdbsum/1nr0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nr0 ProSAT], [http://www.topsan.org/Proteins/NYSGXRC/1nr0 TOPSAN]</span></td></tr>

[[http://www.uniprot.org/uniprot/WDR1_CAEEL WDR1_CAEEL]] Induces disassembly of actin filaments in conjunction with ADF/cofilin family proteins. Regulator of actin organization in myofibrils.

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== Publication Abstract from PubMed ==

Actin-interacting protein 1 (AIP1) is a WD40 repeat protein that enhances actin filament disassembly in the presence of actin-depolymerizing factor (ADF)/cofilin. AIP1 also caps the barbed end of ADF/cofilin-bound actin filament. However, the mechanism by which AIP1 interacts with ADF/cofilin and actin is not clearly understood. We determined the crystal structure of Caenorhabditis elegans AIP1 (UNC-78), which revealed 14 WD40 modules arranged in two seven-bladed beta-propeller domains. The structure allowed for the mapping of conserved surface residues, and mutagenesis studies identified five residues that affected the ADF/cofilin-dependent actin filament disassembly activity. Mutations of these residues, which reside in blades 3 and 4 in the N-terminal propeller domain, had significant effects on the disassembly activity but did not alter the barbed end capping activity. These data support a model in which this conserved surface of AIP1 plays a direct role in enhancing fragmentation/depolymerization of ADF/cofilin-bound actin filaments but not in barbed end capping.

Identification of functional residues on Caenorhabditis elegans actin-interacting protein 1 (UNC-78) for disassembly of actin depolymerizing factor/cofilin-bound actin filaments.,Mohri K, Vorobiev S, Fedorov AA, Almo SC, Ono S J Biol Chem. 2004 Jul 23;279(30):31697-707. Epub 2004 May 18. PMID:15150269<ref>PMID:15150269</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1nr0" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Caeel]]

[[Category: Almo, S C]]

[[Category: Burley, S K]]

[[Category: Mohri, K]]

[[Category: Structural genomic]]

[[Category: Ono, S]]

[[Category: Vorobiev, S M]]

[[Category: Wd40 repeat]]