View source for 2kog


==lipid-bound synaptobrevin solution NMR structure==
<StructureSection load='2kog' size='340' side='right'caption='[[2kog]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2kog]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KOG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KOG FirstGlance]. <br>
</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=2kog FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kog OCA], [https://pdbe.org/2kog PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kog RCSB], [https://www.ebi.ac.uk/pdbsum/2kog PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kog ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VAMP2_RAT VAMP2_RAT] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ko/2kog_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2kog ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The synaptic vesicle protein synaptobrevin engages with syntaxin and SNAP-25 to form the SNARE complex, which drives membrane fusion in neuronal exocytosis. In the SNARE complex, the SNARE motif of synaptobrevin forms a 55-residue helix, but it has been assumed to be mostly unstructured in its prefusion form. NMR data for full-length synaptobrevin in dodecylphosphocholine micelles reveals two transient helical segments flanked by natively disordered regions and a third more stable helix. Transient helix I comprises the most N-terminal part of the SNARE motif, transient helix II extends the SNARE motif into the juxtamembrane region, and the more stable helix III is the transmembrane domain. These helices may have important consequences for SNARE complex folding and fusion: helix I likely forms a nucleation site, the C-terminal disordered SNARE motif may act as a folding arrest signal, and helix II likely couples SNARE complex folding and fusion.

Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation.,Ellena JF, Liang B, Wiktor M, Stein A, Cafiso DS, Jahn R, Tamm LK Proc Natl Acad Sci U S A. 2009 Nov 16. PMID:19918058<ref>PMID:19918058</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 2kog" style="background-color:#fffaf0;"></div>

==See Also==
*[[Vesicle-associated membrane protein 3D structures|Vesicle-associated membrane protein 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Cafiso DS]]
[[Category: Ellena JF]]
[[Category: Jahn R]]
[[Category: Liang B]]
[[Category: Stein A]]
[[Category: Tamm LK]]
[[Category: Wiktor M]]