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2lw9
From Proteopedia
(Difference between revisions)
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| - | + | ==NMR solution structure of Myo10 anti-CC== | |
| - | + | <StructureSection load='2lw9' size='340' side='right' caption='[[2lw9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[2lw9]] is a 2 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=2lw9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lw9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2lw9 RCSB], [http://www.ebi.ac.uk/pdbsum/2lw9 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <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. | ||
| - | + | 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> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | == | + | ==See Also== |
| - | + | *[[Myosin|Myosin]] | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Lu, Q | + | [[Category: Lu, Q]] |
| - | [[Category: Ye, F | + | [[Category: Ye, F]] |
| - | [[Category: Zhang, M | + | [[Category: Zhang, M]] |
[[Category: Motor protein]] | [[Category: Motor protein]] | ||
[[Category: Myo10 anti-cc]] | [[Category: Myo10 anti-cc]] | ||
Revision as of 12:51, 18 December 2014
NMR solution structure of Myo10 anti-CC
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Categories: Homo sapiens | Lu, Q | Ye, F | Zhang, M | Motor protein | Myo10 anti-cc
