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| | <StructureSection load='3rl0' size='340' side='right'caption='[[3rl0]], [[Resolution|resolution]] 3.80Å' scene=''> | | <StructureSection load='3rl0' size='340' side='right'caption='[[3rl0]], [[Resolution|resolution]] 3.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rl0]] is a 40 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RL0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rl0]] is a 40 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RL0 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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.8Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3rk2|3rk2]], [[3rk3|3rk3]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VAMP2, SYB2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Stx1a, Sap ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), SNAP25, SNAP ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CPLX1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3rl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rl0 OCA], [https://pdbe.org/3rl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rl0 RCSB], [https://www.ebi.ac.uk/pdbsum/3rl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rl0 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=3rl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rl0 OCA], [https://pdbe.org/3rl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rl0 RCSB], [https://www.ebi.ac.uk/pdbsum/3rl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rl0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SNP25_HUMAN SNP25_HUMAN]] t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. [[https://www.uniprot.org/uniprot/VAMP2_HUMAN VAMP2_HUMAN]] Involved in the targeting and/or fusion of transport vesicles to their target membrane. [[https://www.uniprot.org/uniprot/STX1A_RAT STX1A_RAT]] Potentially involved in docking of synaptic vesicles at presynaptic active zones. May play a critical role in neurotransmitter exocytosis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. [[https://www.uniprot.org/uniprot/CPLX1_HUMAN CPLX1_HUMAN]] Positively regulates a late step in synaptic vesicle exocytosis. Organizes the SNAREs into a cross-linked zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion, thereby preventing SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. Also involved in glucose-induced secretion of insulin by pancreatic beta-cells (By similarity).
| + | [https://www.uniprot.org/uniprot/SNP25_HUMAN SNP25_HUMAN] t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | *[[Synaptosomal-associated protein|Synaptosomal-associated protein]] | | *[[Synaptosomal-associated protein|Synaptosomal-associated protein]] |
| | *[[Syntaxin 3D structures|Syntaxin 3D structures]] | | *[[Syntaxin 3D structures|Syntaxin 3D structures]] |
| - | *[[Vesicle-associated membrane protein|Vesicle-associated membrane protein]] | + | *[[Vesicle-associated membrane protein 3D structures|Vesicle-associated membrane protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Buffalo rat]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Human]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Kuemmel, D]] | + | [[Category: Rattus norvegicus]] |
| - | [[Category: Reinisch, K M]] | + | [[Category: Kuemmel D]] |
| - | [[Category: Membrane fusion]] | + | [[Category: Reinisch KM]] |
| - | [[Category: Membrane protein-exocytosis complex]]
| + | |
| - | [[Category: Snare protein]]
| + | |
| Structural highlights
Function
SNP25_HUMAN t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF.
Publication Abstract from PubMed
Complexin prevents SNAREs from releasing neurotransmitters until an action potential arrives at the synapse. To understand the mechanism for this inhibition, we determined the structure of complexin bound to a mimetic of a prefusion SNAREpin lacking the portion of the v-SNARE that zippers last to trigger fusion. The 'central helix' of complexin is anchored to one SNARE complex, while its 'accessory helix' extends away at ~45 degrees and bridges to a second complex, occupying the vacant v-SNARE binding site to inhibit fusion. We expected the accessory helix to compete with the v-SNARE for t-SNARE binding but found instead that the interaction occurs intermolecularly. Thus, complexin organizes the SNAREs into a zigzag topology that, when interposed between the vesicle and plasma membranes, is incompatible with fusion.
Complexin cross-links prefusion SNAREs into a zigzag array.,Kummel D, Krishnakumar SS, Radoff DT, Li F, Giraudo CG, Pincet F, Rothman JE, Reinisch KM Nat Struct Mol Biol. 2011 Jul 24;18(8):927-33. doi: 10.1038/nsmb.2101. PMID:21785414[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kummel D, Krishnakumar SS, Radoff DT, Li F, Giraudo CG, Pincet F, Rothman JE, Reinisch KM. Complexin cross-links prefusion SNAREs into a zigzag array. Nat Struct Mol Biol. 2011 Jul 24;18(8):927-33. doi: 10.1038/nsmb.2101. PMID:21785414 doi:10.1038/nsmb.2101
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