1l4a: Difference between revisions
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<StructureSection load='1l4a' size='340' side='right'caption='[[1l4a]], [[Resolution|resolution]] 2.95Å' scene=''> | <StructureSection load='1l4a' size='340' side='right'caption='[[1l4a]], [[Resolution|resolution]] 2.95Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1l4a]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4A OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[1l4a]] is a 5 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L4A FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1sfc|1sfc]], [[1kil|1kil]]</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;'>[[1sfc|1sfc]], [[1kil|1kil]]</div></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=1l4a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4a OCA], [https://pdbe.org/1l4a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l4a RCSB], [https://www.ebi.ac.uk/pdbsum/1l4a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l4a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/SYB_DORPE SYB_DORPE]] Intrinsic membrane protein of small synaptic vesicles. [[https://www.uniprot.org/uniprot/CPLX_DORPE CPLX_DORPE]] Positively regulates a late step in synaptic vesicle exocytosis. | ||
== 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]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:39, 18 August 2021
X-RAY STRUCTURE OF THE NEURONAL COMPLEXIN/SNARE COMPLEX FROM THE SQUID LOLIGO PEALEIX-RAY STRUCTURE OF THE NEURONAL COMPLEXIN/SNARE COMPLEX FROM THE SQUID LOLIGO PEALEI
Structural highlights
Function[SYB_DORPE] Intrinsic membrane protein of small synaptic vesicles. [CPLX_DORPE] Positively regulates a late step in synaptic vesicle exocytosis. 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 PubMedNerve terminals release neurotransmitters from vesicles into the synaptic cleft upon transient increases in intracellular Ca(2+). This exocytotic process requires the formation of trans SNARE complexes and is regulated by accessory proteins including the complexins. Here we report the crystal structure of a squid core complexin-SNARE complex at 2.95-A resolution. A helical segment of complexin binds in anti-parallel fashion to the four-helix bundle of the core SNARE complex and interacts at its C terminus with syntaxin and synaptobrevin around the ionic zero layer of the SNARE complex. We propose that this structure is part of a multiprotein fusion machinery that regulates vesicle fusion at a late pre-fusion stage. Accordingly, Ca(2+) may initiate membrane fusion by acting directly or indirectly on complexin, thus allowing the conformational transitions of the trans SNARE complex that are thought to drive membrane fusion. X-ray structure of a neuronal complexin-SNARE complex from squid.,Bracher A, Kadlec J, Betz H, Weissenhorn W J Biol Chem. 2002 Jul 19;277(29):26517-23. Epub 2002 May 9. PMID:12004067[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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