3ipd: Difference between revisions
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==Helical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21== | ==Helical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21== | ||
<StructureSection load='3ipd' size='340' side='right' caption='[[3ipd]], [[Resolution|resolution]] 4.80Å' scene=''> | <StructureSection load='3ipd' size='340' side='right'caption='[[3ipd]], [[Resolution|resolution]] 4.80Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3ipd]] is a 8 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3ipd]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=3hd9 3hd9]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IPD FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3hd7|3hd7]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3hd7|3hd7]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Vamp2 ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Vamp2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), Stx1a ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat]), SNAP-25 SPLICE VARIANT A ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3ipd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ipd OCA], [https://pdbe.org/3ipd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ipd RCSB], [https://www.ebi.ac.uk/pdbsum/3ipd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ipd ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[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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*[[Synaptosomal-associated protein|Synaptosomal-associated protein]] | *[[Synaptosomal-associated protein|Synaptosomal-associated protein]] | ||
*[[Syntaxin|Syntaxin]] | *[[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 == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Buffalo rat]] | [[Category: Buffalo rat]] | ||
[[Category: Large Structures]] | |||
[[Category: Jahn, R]] | [[Category: Jahn, R]] | ||
[[Category: Stein, A]] | [[Category: Stein, A]] | ||
Revision as of 06:38, 21 April 2022
Helical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21Helical extension of the neuronal SNARE complex into the membrane, spacegroup I 21 21 21
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 PubMedNeurotransmission relies on synaptic vesicles fusing with the membrane of nerve cells to release their neurotransmitter content into the synaptic cleft, a process requiring the assembly of several members of the SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) family. SNAREs represent an evolutionarily conserved protein family that mediates membrane fusion in the secretory and endocytic pathways of eukaryotic cells. On membrane contact, these proteins assemble in trans between the membranes as a bundle of four alpha-helices, with the energy released during assembly being thought to drive fusion. However, it is unclear how the energy is transferred to the membranes and whether assembly is conformationally linked to fusion. Here, we report the X-ray structure of the neuronal SNARE complex, consisting of rat syntaxin 1A, SNAP-25 and synaptobrevin 2, with the carboxy-terminal linkers and transmembrane regions at 3.4 A resolution. The structure shows that assembly proceeds beyond the already known core SNARE complex, resulting in a continuous helical bundle that is further stabilized by side-chain interactions in the linker region. Our results suggest that the final phase of SNARE assembly is directly coupled to membrane merger. Helical extension of the neuronal SNARE complex into the membrane.,Stein A, Weber G, Wahl MC, Jahn R Nature. 2009 Jul 23;460(7254):525-8. Epub 2009 Jul 1. PMID:19571812[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Buffalo rat
- Large Structures
- Jahn, R
- Stein, A
- Wahl, M C
- Weber, G
- 4-helical bundle
- Acetylation
- Alternative splicing
- Cell junction
- Cell membrane
- Coiled coil
- Cytoplasm
- Cytoplasmic vesicle
- Exocytosis
- Lipoprotein
- Membrane
- Membrane fusion
- Membrane protein
- Neurotransmitter transport
- Palmitate
- Phosphoprotein
- Synapse
- Synaptosome
- Transmembrane
- Transport
- Transport protein