3swh

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Current revision (09:57, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3swh' size='340' side='right'caption='[[3swh]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='3swh' size='340' side='right'caption='[[3swh]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3swh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SWH FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3swh]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SWH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SWH FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Unc13a, Unc13h1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.65&#8491;</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=3swh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3swh OCA], [https://pdbe.org/3swh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3swh RCSB], [https://www.ebi.ac.uk/pdbsum/3swh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3swh ProSAT]</span></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=3swh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3swh OCA], [https://pdbe.org/3swh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3swh RCSB], [https://www.ebi.ac.uk/pdbsum/3swh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3swh ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/UN13A_RAT UN13A_RAT]] Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. Also involved in secretory granule priming in insulin secretion.<ref>PMID:9697857</ref> <ref>PMID:11343654</ref> <ref>PMID:11792326</ref>
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[https://www.uniprot.org/uniprot/UN13A_RAT UN13A_RAT] Plays a role in vesicle maturation during exocytosis as a target of the diacylglycerol second messenger pathway. Involved in neurotransmitter release by acting in synaptic vesicle priming prior to vesicle fusion and participates in the activity-dependent refilling of readily releasable vesicle pool (RRP). Essential for synaptic vesicle maturation in most excitatory/glutamatergic but not inhibitory/GABA-mediated synapses. Also involved in secretory granule priming in insulin secretion.<ref>PMID:9697857</ref> <ref>PMID:11343654</ref> <ref>PMID:11792326</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Unc13/Munc13s play a crucial function in neurotransmitter release through their MUN domain, which mediates the transition from the Syntaxin-1/Munc18-1 complex to the SNARE complex. The MUN domain was suggested to be related to tethering factors, but no MUN-domain structure is available to experimentally validate this notion and address key unresolved questions about the interactions and minimal structural unit required for Unc13/Munc13 function. Here we identify an autonomously folded module within the MUN domain (MUN-CD) and show that its crystal structure is remarkably similar to several tethering factors. We also show that the activity in promoting the Syntaxin-1/Munc18-1 to SNARE complex transition is strongly impaired in MUN-CD. These results show that MUN domains and tethering factors indeed belong to the same family and may have a common role in membrane trafficking. We propose a model whereby the MUN-CD module is central for Munc13 function but full activity requires adjacent sequences.
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The Crystal Structure of a Munc13 C-terminal Module Exhibits a Remarkable Similarity to Vesicle Tethering Factors.,Li W, Ma C, Guan R, Xu Y, Tomchick DR, Rizo J Structure. 2011 Oct 12;19(10):1443-55. PMID:22000513<ref>PMID:22000513</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3swh" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Buffalo rat]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Li, W]]
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[[Category: Rattus norvegicus]]
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[[Category: Rizo, J]]
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[[Category: Li W]]
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[[Category: Tomchick, D R]]
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[[Category: Rizo J]]
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[[Category: Alpha helical]]
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[[Category: Tomchick DR]]
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[[Category: Exocytosis]]
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[[Category: Neurotransmitter release]]
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[[Category: Snare motif]]
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Current revision

Munc13-1, MUN domain, C-terminal module

PDB ID 3swh

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