2lw9

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==NMR solution structure of Myo10 anti-CC==
==NMR solution structure of Myo10 anti-CC==
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<StructureSection load='2lw9' size='340' side='right' caption='[[2lw9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2lw9' size='340' side='right'caption='[[2lw9]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2lw9]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LW9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2LW9 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2lw9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LW9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LW9 FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO10, KIAA0799 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<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=2lw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lw9 OCA], [http://pdbe.org/2lw9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2lw9 RCSB], [http://www.ebi.ac.uk/pdbsum/2lw9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2lw9 ProSAT]</span></td></tr>
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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=2lw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lw9 OCA], [https://pdbe.org/2lw9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lw9 RCSB], [https://www.ebi.ac.uk/pdbsum/2lw9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lw9 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/MYO10_HUMAN MYO10_HUMAN]] 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 plus end-directed motor. 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. May play a role in neurite outgrowth and axon guidance. Plays a role in formation of the podosome belt in osteoclasts (By similarity).<ref>PMID:16894163</ref>
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[https://www.uniprot.org/uniprot/MYO10_HUMAN MYO10_HUMAN] 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 plus end-directed motor. 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. May play a role in neurite outgrowth and axon guidance. Plays a role in formation of the podosome belt in osteoclasts (By similarity).<ref>PMID:16894163</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Processive movements of unconventional myosins on actin filaments generally require motor dimerization. A commonly accepted myosin dimerization mechanism is via formation of a parallel coiled-coil dimer by a stretch of amino acid residues immediately carboxyl-terminal to the motor's lever-arm domain. Here, we discover that the predicted coiled-coil region of myosin X forms a highly stable, antiparallel coiled-coil dimer (anti-CC). Disruption of the anti-CC either by single-point mutations or by replacement of the anti-CC with a parallel coiled coil with a similar length compromised the filopodial induction activity of myosin X. We further show that the anti-CC and the single alpha-helical domain of myosin X are connected by a semirigid helical linker. The anti-CC-mediated dimerization may enable myosin X to walk on both single and bundled actin filaments.
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Antiparallel coiled-coil-mediated dimerization of myosin X.,Lu Q, Ye F, Wei Z, Wen Z, Zhang M Proc Natl Acad Sci U S A. 2012 Oct 23;109(43):17388-93. doi:, 10.1073/pnas.1208642109. Epub 2012 Sep 10. PMID:23012428<ref>PMID:23012428</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 2lw9" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
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*[[Myosin|Myosin]]
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*[[Myosin 3D Structures|Myosin 3D Structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Lu, Q]]
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[[Category: Large Structures]]
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[[Category: Ye, F]]
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[[Category: Lu Q]]
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[[Category: Zhang, M]]
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[[Category: Ye F]]
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[[Category: Motor protein]]
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[[Category: Zhang M]]
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[[Category: Myo10 anti-cc]]
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Current revision

NMR solution structure of Myo10 anti-CC

PDB ID 2lw9

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