5b86

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'''Unreleased structure'''
 
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The entry 5b86 is ON HOLD until Paper Publication
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==Crystal structure of M-Sec==
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<StructureSection load='5b86' size='340' side='right' caption='[[5b86]], [[Resolution|resolution]] 3.02&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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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=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>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/TNAP2_MOUSE TNAP2_MOUSE]] May play a role as a mediator of inflammation and angiogenesis.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5b86" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Fukai, S]]
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[[Category: Sato, Y]]
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[[Category: Yamagata, A]]
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[[Category: Yamashita, M]]
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[[Category: Exocyst complex]]
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[[Category: Exocytosis]]
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[[Category: Helical protein]]
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[[Category: Immune system]]
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[[Category: Membrane traffic]]

Revision as of 17:36, 19 October 2016

Crystal structure of M-Sec

5b86, resolution 3.02Å

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