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| | ==NMR solution structure of Myo10 anti-CC== | | ==NMR solution structure of Myo10 anti-CC== |
| - | <StructureSection load='2lw9' size='340' side='right'caption='[[2lw9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2lw9' size='340' side='right'caption='[[2lw9]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2lw9]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2LW9 FirstGlance]. <br> | + | <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> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MYO10, KIAA0799 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><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> |
| - | <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 == |
| - | [[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>
| + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lu, Q]] | + | [[Category: Lu Q]] |
| - | [[Category: Ye, F]] | + | [[Category: Ye F]] |
| - | [[Category: Zhang, M]] | + | [[Category: Zhang M]] |
| - | [[Category: Motor protein]]
| + | |
| - | [[Category: Myo10 anti-cc]]
| + | |
| Structural highlights
Function
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).[1]
Publication Abstract from PubMed
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.
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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bohil AB, Robertson BW, Cheney RE. Myosin-X is a molecular motor that functions in filopodia formation. Proc Natl Acad Sci U S A. 2006 Aug 15;103(33):12411-6. Epub 2006 Aug 7. PMID:16894163 doi:10.1073/pnas.0602443103
- ↑ Lu Q, Ye F, Wei Z, Wen Z, Zhang M. Antiparallel coiled-coil-mediated dimerization of myosin X. 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 doi:10.1073/pnas.1208642109
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