3rl0
From Proteopedia
(Difference between revisions)
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==Truncated SNARE complex with complexin (P1)== | ==Truncated SNARE complex with complexin (P1)== | ||
<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 [http://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[3rl0]] is a 40 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat] and [http://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 [http://oca.weizmann.ac.il/oca-docs/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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rk2|3rk2]], [[3rk3|3rk3]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rk2|3rk2]], [[3rk3|3rk3]]</td></tr> | ||
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VAMP2, SYB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">VAMP2, SYB2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Stx1a, Sap ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), SNAP25, SNAP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CPLX1 ([http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3rl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rl0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3rl0 RCSB], [http://www.ebi.ac.uk/pdbsum/3rl0 PDBsum]</span></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=3rl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rl0 OCA], [http://pdbe.org/3rl0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3rl0 RCSB], [http://www.ebi.ac.uk/pdbsum/3rl0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3rl0 ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[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_HUMAN VAMP2_HUMAN]] Involved in the targeting and/or fusion of transport vesicles to their target membrane. [[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/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_HUMAN VAMP2_HUMAN]] Involved in the targeting and/or fusion of transport vesicles to their target membrane. [[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/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). |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
+ | <div class="pdbe-citations 3rl0" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
- | [[Category: | + | [[Category: Buffalo rat]] |
- | [[Category: | + | [[Category: Human]] |
[[Category: Kuemmel, D]] | [[Category: Kuemmel, D]] | ||
[[Category: Reinisch, K M]] | [[Category: Reinisch, K M]] |
Revision as of 04:26, 5 August 2016
Truncated SNARE complex with complexin (P1)
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