1io0: Difference between revisions

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<StructureSection load='1io0' size='340' side='right' caption='[[1io0]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
<StructureSection load='1io0' size='340' side='right' caption='[[1io0]], [[Resolution|resolution]] 1.45&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<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>
<table><tr><td colspan='2'>[[1io0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Chick Chick]. 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>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=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>
<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=1io0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io0 OCA], [http://pdbe.org/1io0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1io0 RCSB], [http://www.ebi.ac.uk/pdbsum/1io0 PDBsum]</span></td></tr>
</table>
</table>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 1io0" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Gallus gallus]]
[[Category: Chick]]
[[Category: Kostyukova, A]]
[[Category: Kostyukova, A]]
[[Category: Krieger, I]]
[[Category: Krieger, I]]

Revision as of 12:05, 10 September 2015

CRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALFCRYSTAL STRUCTURE OF TROPOMODULIN C-TERMINAL HALF

Structural highlights

1io0 is a 1 chain structure with sequence from Chick. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Krieger I, Kostyukova A, Yamashita A, Nitanai Y, Maeda Y. Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping. Biophys J. 2002 Nov;83(5):2716-25. PMID:12414704

1io0, resolution 1.45Å

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OCA