2n1t

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==Dynamic binding mode of a synaptotagmin-1-SNARE complex in solution==
==Dynamic binding mode of a synaptotagmin-1-SNARE complex in solution==
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<StructureSection load='2n1t' size='340' side='right' caption='[[2n1t]], [[NMR_Ensembles_of_Models | 5 NMR models]]' scene=''>
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<StructureSection load='2n1t' size='340' side='right'caption='[[2n1t]], [[NMR_Ensembles_of_Models | 5 NMR models]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2n1t]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N1T FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2n1t]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1T FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sfc|1sfc]], [[1uow|1uow]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sfc|1sfc]], [[1uow|1uow]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Syb2, Vamp2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Sap, Stx1a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), SNAP, SNAP25, SNAP-25A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SVP65, SYT, SYT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Syb2, Vamp2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Sap, Stx1a ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), SNAP, SNAP25, SNAP-25A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), SVP65, SYT, SYT1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2n1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1t OCA], [http://pdbe.org/2n1t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n1t RCSB], [http://www.ebi.ac.uk/pdbsum/2n1t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1t ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n1t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1t OCA], [https://pdbe.org/2n1t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1t RCSB], [https://www.ebi.ac.uk/pdbsum/2n1t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1t ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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. [[http://www.uniprot.org/uniprot/VAMP2_RAT VAMP2_RAT]] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). [[http://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. [[http://www.uniprot.org/uniprot/SYT1_HUMAN SYT1_HUMAN]] May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
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[[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_RAT VAMP2_RAT]] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). [[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/SYT1_HUMAN SYT1_HUMAN]] May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca(2+)-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca(2+)-independent manner; these are neurexins, syntaxin and AP2.
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Synaptosomal-associated protein|Synaptosomal-associated protein]]
*[[Synaptosomal-associated protein|Synaptosomal-associated protein]]
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*[[Synaptotagmin|Synaptotagmin]]
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*[[Synaptotagmin 3D structures|Synaptotagmin 3D structures]]
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*[[Syntaxin|Syntaxin]]
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*[[Syntaxin 3D structures|Syntaxin 3D structures]]
*[[Vesicle-associated membrane protein|Vesicle-associated membrane protein]]
*[[Vesicle-associated membrane protein|Vesicle-associated membrane protein]]
== References ==
== References ==
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[[Category: Buffalo rat]]
[[Category: Buffalo rat]]
[[Category: Human]]
[[Category: Human]]
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[[Category: Large Structures]]
[[Category: Bacaj, T]]
[[Category: Bacaj, T]]
[[Category: Barlow, N]]
[[Category: Barlow, N]]

Revision as of 15:25, 2 June 2021

Dynamic binding mode of a synaptotagmin-1-SNARE complex in solution

PDB ID 2n1t

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