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| | <StructureSection load='1sfc' size='340' side='right'caption='[[1sfc]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='1sfc' size='340' side='right'caption='[[1sfc]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1sfc]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. The November 2013 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''SNARE Proteins'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2013_11 10.2210/rcsb_pdb/mom_2013_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1SFC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1sfc]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. The November 2013 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''SNARE Proteins'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2013_11 10.2210/rcsb_pdb/mom_2013_11]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SFC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MPD:(4S)-2-METHYL-2,4-PENTANEDIOL'>MPD</scene>, <scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></td></tr> |
| - | <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=1sfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sfc OCA], [http://pdbe.org/1sfc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sfc RCSB], [http://www.ebi.ac.uk/pdbsum/1sfc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sfc 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=1sfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sfc OCA], [https://pdbe.org/1sfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sfc RCSB], [https://www.ebi.ac.uk/pdbsum/1sfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sfc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SNP25_RAT SNP25_RAT]] 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. | + | [[https://www.uniprot.org/uniprot/SNP25_RAT SNP25_RAT]] 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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | ==See Also== | | ==See Also== |
| - | *[[Syntaxin|Syntaxin]] | + | *[[Syntaxin 3D structures|Syntaxin 3D structures]] |
| | *[[Vesicle-associated membrane protein|Vesicle-associated membrane protein]] | | *[[Vesicle-associated membrane protein|Vesicle-associated membrane protein]] |
| | == References == | | == References == |
| Structural highlights
Function
[SNP25_RAT] 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. [VAMP2_RAT] Involved in the targeting and/or fusion of transport vesicles to their target membrane (By similarity). [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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The evolutionarily conserved SNARE proteins and their complexes are involved in the fusion of vesicles with their target membranes; however, the overall organization and structural details of these complexes are unknown. Here we report the X-ray crystal structure at 2.4 A resolution of a core synaptic fusion complex containing syntaxin-1 A, synaptobrevin-II and SNAP-25B. The structure reveals a highly twisted and parallel four-helix bundle that differs from the bundles described for the haemagglutinin and HIV/SIV gp41 membrane-fusion proteins. Conserved leucine-zipper-like layers are found at the centre of the synaptic fusion complex. Embedded within these leucine-zipper layers is an ionic layer consisting of an arginine and three glutamine residues contributed from each of the four alpha-helices. These residues are highly conserved across the entire SNARE family. The regions flanking the leucine-zipper-like layers contain a hydrophobic core similar to that of more general four-helix-bundle proteins. The surface of the synaptic fusion complex is highly grooved and possesses distinct hydrophilic, hydrophobic and charged regions. These characteristics may be important for membrane fusion and for the binding of regulatory factors affecting neurotransmission.
Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution.,Sutton RB, Fasshauer D, Jahn R, Brunger AT Nature. 1998 Sep 24;395(6700):347-53. PMID:9759724[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sutton RB, Fasshauer D, Jahn R, Brunger AT. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution. Nature. 1998 Sep 24;395(6700):347-53. PMID:9759724 doi:http://dx.doi.org/10.1038/26412
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