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1io0

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[[Image:1io0.png|left|200px]]
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==CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF==
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<StructureSection load='1io0' size='340' side='right' caption='[[1io0]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1io0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IO0 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1io0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1io0 RCSB], [http://www.ebi.ac.uk/pdbsum/1io0 PDBsum]</span></td></tr>
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<table>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/io/1io0_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Tropomodulin is the unique pointed-end capping protein of the actin-tropomyosin filament. By blocking elongation and depolymerization, tropomodulin regulates the architecture and the dynamics of the filament. Here we report the crystal structure at 1.45-A resolution of the C-terminal half of tropomodulin (C20), the actin-binding moiety of tropomodulin. C20 is a leucine-rich repeat domain, and this is the first actin-associated protein with a leucine-rich repeat. Binding assays suggested that C20 also interacts with the N-terminal fragment, M1-M2-M3, of nebulin. Based on the crystal structure, we propose a model for C20 docking to the actin subunit at the pointed end. Although speculative, the model is consistent with the idea that a tropomodulin molecule competes with an actin subunit for a pointed end. The model also suggests that interactions with tropomyosin, actin, and nebulin are all possible sources of influences on the dynamic properties of pointed-end capping by tropomodulin.
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{{STRUCTURE_1io0| PDB=1io0 | SCENE= }}
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Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping.,Krieger I, Kostyukova A, Yamashita A, Nitanai Y, Maeda Y Biophys J. 2002 Nov;83(5):2716-25. PMID:12414704<ref>PMID:12414704</ref>
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===CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF===
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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{{ABSTRACT_PUBMED_12414704}}
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== References ==
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<references/>
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==About this Structure==
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__TOC__
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[[1io0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO0 OCA].
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</StructureSection>
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==Reference==
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<ref group="xtra">PMID:012414704</ref><ref group="xtra">PMID:015211521</ref><references group="xtra"/>
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Kostyukova, A.]]
[[Category: Kostyukova, A.]]

Revision as of 13:52, 28 September 2014

CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF

1io0, resolution 1.45Å

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