5b86
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of M-Sec== | |
| + | <StructureSection load='5b86' size='340' side='right' caption='[[5b86]], [[Resolution|resolution]] 3.02Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5b86]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5B86 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5B86 FirstGlance]. <br> | ||
| + | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5b86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5b86 OCA], [http://pdbe.org/5b86 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5b86 RCSB], [http://www.ebi.ac.uk/pdbsum/5b86 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5b86 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/TNAP2_MOUSE TNAP2_MOUSE]] May play a role as a mediator of inflammation and angiogenesis. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The tunneling nanotube (TNT) is a structure used for intercellular communication, and is a thin membrane protrusion mediating transport of various signaling molecules and cellular components. M-Sec has potent membrane deformation ability and induces TNT formation in cooperation with the Ral/exocyst complex. Here, we show that the N-terminal polybasic region of M-Sec directly binds phosphatidylinositol (4,5)-bisphosphate for its localization to the plasma membrane during the initial stage of TNT formation. We further report a crystal structure of M-Sec, which consists of helix bundles arranged in a straight rod-like shape, similar to the membrane tethering complex subunits. A positively charged surface in the C-terminal domains is required for M-Sec interaction with active RalA to extend the plasma membrane protrusions. Our results suggest that the membrane-associated M-Sec recruits active RalA, which directs the exocyst complex to form TNTs. | ||
| - | + | Distinct Roles for the N- and C-terminal Regions of M-Sec in Plasma Membrane Deformation during Tunneling Nanotube Formation.,Kimura S, Yamashita M, Yamakami-Kimura M, Sato Y, Yamagata A, Kobashigawa Y, Inagaki F, Amada T, Hase K, Iwanaga T, Ohno H, Fukai S Sci Rep. 2016 Sep 15;6:33548. doi: 10.1038/srep33548. PMID:27629377<ref>PMID:27629377</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 5b86" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Fukai, S]] | ||
| + | [[Category: Sato, Y]] | ||
| + | [[Category: Yamagata, A]] | ||
| + | [[Category: Yamashita, M]] | ||
| + | [[Category: Exocyst complex]] | ||
| + | [[Category: Exocytosis]] | ||
| + | [[Category: Helical protein]] | ||
| + | [[Category: Immune system]] | ||
| + | [[Category: Membrane traffic]] | ||
Revision as of 17:36, 19 October 2016
Crystal structure of M-Sec
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