3tfm

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[[Image:3tfm.jpg|left|200px]]
 
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==Myosin X PH1N-PH2-PH1C tandem==
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The line below this paragraph, containing "STRUCTURE_3tfm", creates the "Structure Box" on the page.
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<StructureSection load='3tfm' size='340' side='right'caption='[[3tfm]], [[Resolution|resolution]] 2.53&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3tfm]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TFM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TFM FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.53&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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{{STRUCTURE_3tfm| PDB=3tfm | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3tfm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tfm OCA], [https://pdbe.org/3tfm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tfm RCSB], [https://www.ebi.ac.uk/pdbsum/3tfm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tfm ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MYO10_RAT MYO10_RAT] Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. MYO10 binds to actin filaments and actin bundles and functions as a plus end-directed motor. Moves with higher velocity and takes larger steps on actin bundles than on single actin filaments (By similarity). The tail domain binds to membranous compartments containing phosphatidylinositol 3,4,5-trisphosphate or integrins, and mediates cargo transport along actin filaments. Regulates cell shape, cell spreading and cell adhesion. Stimulates the formation and elongation of filopodia. In hippocampal neurons it induces the formation of dendritic filopodia by trafficking the actin-remodeling protein VASP to the tips of filopodia, where it promotes actin elongation. Plays a role in formation of the podosome belt in osteoclasts (By similarity).[UniProtKB:Q9HD67]<ref>PMID:21965296</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Myosin X (MyoX) is an unconventional myosin that is known to induce the formation and elongation of filopodia in many cell types. MyoX-induced filopodial induction requires the three PH domains in its tail region, although with unknown underlying molecular mechanisms. MyoX's first PH domain is split into halves by its second PH domain. We show here that the PH1(N)-PH2-PH1(C) tandem allows MyoX to bind to phosphatidylinositol (3,4,5)-triphosphate [PI(3,4,5)P(3)] with high specificity and cooperativity. We further show that PH2 is responsible for the specificity of the PI(3,4,5)P(3) interaction, whereas PH1 functions to enhance the lipid membrane-binding avidity of the tandem. The structure of the MyoX PH1(N)-PH2-PH1(C) tandem reveals that the split PH1, PH2, and the highly conserved interdomain linker sequences together form a rigid supramodule with two lipid-binding pockets positioned side by side for binding to phosphoinositide membrane bilayers with cooperativity. Finally, we demonstrate that disruption of PH2-mediated binding to PI(3,4,5)P(3) abolishes MyoX's function in inducing filopodial formation and elongation.
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===Myosin X PH1N-PH2-PH1C tandem===
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Structural basis of the myosin X PH1N-PH2-PH1C tandem as a specific and acute cellular PI(3,4,5)P3 sensor.,Lu Q, Yu J, Yan J, Wei Z, Zhang M Mol Biol Cell. 2011 Nov;22(22):4268-78. Epub 2011 Sep 30. PMID:21965296<ref>PMID:21965296</ref>
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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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<div class="pdbe-citations 3tfm" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_21965296}}, adds the Publication Abstract to the page
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*[[Myosin 3D Structures|Myosin 3D Structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 21965296 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_21965296}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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[[3tfm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TFM OCA].
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==Reference==
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<ref group="xtra">PMID:021965296</ref><references group="xtra"/>
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Lu, Q.]]
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[[Category: Lu Q]]
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[[Category: Wei, Z.]]
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[[Category: Wei Z]]
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[[Category: Yan, J.]]
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[[Category: Yan J]]
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[[Category: Yu, J.]]
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[[Category: Yu J]]
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[[Category: Zhang, M.]]
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[[Category: Zhang M]]
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[[Category: Motor protein]]
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[[Category: Split ph domain]]
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Current revision

Myosin X PH1N-PH2-PH1C tandem

PDB ID 3tfm

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