2lw9
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<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> | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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;"> | ||
| - | == 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. | ||
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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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2lw9" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
Current revision
NMR solution structure of Myo10 anti-CC
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Categories: Homo sapiens | Large Structures | Lu Q | Ye F | Zhang M
