1t2l

<StructureSection load='1t2l' size='340' side='right' caption='[[1t2l]], [[Resolution|resolution]] 2.80&Aring;' scene=''>

<table><tr><td colspan='2'>[[1t2l]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T2L OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T2L FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=1t2l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t2l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1t2l RCSB], [http://www.ebi.ac.uk/pdbsum/1t2l PDBsum]</span></td></tr>

[[http://www.uniprot.org/uniprot/COTL1_HUMAN COTL1_HUMAN]] Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization.<ref>PMID:11583571</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/t2/1t2l_consurf.spt"</scriptWhenChecked>

</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].

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== Publication Abstract from PubMed ==

Human coactosin-like protein is an actin filament binding protein but does not bind to globular actin. It associates with 5-Lipoxygenase both in vivo and in vitro, playing important roles in modulating the activities of actin and 5-Lipoxygenase. Coactosin counteracts the capping activity of capping protein which inhibits the actin polymerization. We determined the crystal structures of human coactosin-like protein by multi-wavelength anomalous dispersion method. The structure showed a high level of similarity to ADF-H domain, although their amino acid sequences share low degree of homology. A few conserved hydrophobic residues that may contribute to the folding were identified. This structure suggests coactosin-like protein bind to F-actin in a different way from ADF/Cofilin family. Combined with the information from previous mutagenesis studies, the binding sites for F-actin and 5-Lipoxygenase were analyzed, respectively. These two sites are quite close, which might prevent F-actin and 5-Lipoxygenase from binding to coactosin simultaneously.

Crystal structure of human coactosin-like protein.,Liu L, Wei Z, Wang Y, Wan M, Cheng Z, Gong W J Mol Biol. 2004 Nov 19;344(2):317-23. PMID:15522287<ref>PMID:15522287</ref>

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

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[[Category: Chen, Z]]

[[Category: Gong, W]]

[[Category: Liu, L]]

[[Category: Wang, Y]]

[[Category: Wei, Z]]

[[Category: Protein binding]]