3puk: Difference between revisions
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==Re-refinement of the crystal structure of Munc18-3 and Syntaxin4 N-peptide complex== | ==Re-refinement of the crystal structure of Munc18-3 and Syntaxin4 N-peptide complex== | ||
<StructureSection load='3puk' size='340' side='right' caption='[[3puk]], [[Resolution|resolution]] 3.05Å' scene=''> | <StructureSection load='3puk' size='340' side='right'caption='[[3puk]], [[Resolution|resolution]] 3.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3puk]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[3puk]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2pjx 2pjx]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PUK FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2pjx|2pjx]], [[3puj|3puj]]</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;'>[[2pjx|2pjx]], [[3puj|3puj]]</div></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Stxbp3, Stxbp3a, Unc18c ([ | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Stxbp3, Stxbp3a, Unc18c ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=3puk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3puk OCA], [https://pdbe.org/3puk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3puk RCSB], [https://www.ebi.ac.uk/pdbsum/3puk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3puk ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/STXB3_MOUSE STXB3_MOUSE]] Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes.<ref>PMID:9045631</ref> [[https://www.uniprot.org/uniprot/STX4_MOUSE STX4_MOUSE]] Plasma membrane t-SNARE that mediates docking of transport vesicles. Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane. Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones.<ref>PMID:9045631</ref> <ref>PMID:10394363</ref> <ref>PMID:18827011</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 3puk" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 3puk" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Syntaxin-binding protein|Syntaxin-binding protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lk3 transgenic mice]] | [[Category: Lk3 transgenic mice]] | ||
[[Category: Christie, M P]] | [[Category: Christie, M P]] | ||
Revision as of 11:55, 25 May 2022
Re-refinement of the crystal structure of Munc18-3 and Syntaxin4 N-peptide complexRe-refinement of the crystal structure of Munc18-3 and Syntaxin4 N-peptide complex
Structural highlights
Function[STXB3_MOUSE] Together with STX4 and VAMP2, may play a role in insulin-dependent movement of GLUT4 and in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes.[1] [STX4_MOUSE] Plasma membrane t-SNARE that mediates docking of transport vesicles. Necessary for the translocation of SLC2A4 from intracellular vesicles to the plasma membrane. Together with STXB3 and VAMP2, may also play a role in docking/fusion of intracellular GLUT4-containing vesicles with the cell surface in adipocytes and in docking of synaptic vesicles at presynaptic active zones.[2] [3] [4] Publication Abstract from PubMedMunc18-1 and Syntaxin1 are essential proteins for SNARE-mediated neurotransmission. Munc18-1 participates in synaptic vesicle fusion via dual roles: as a docking/chaperone protein by binding closed Syntaxin1, and as a fusion protein that binds SNARE complexes in a Syntaxin1 N-peptide dependent manner. The two roles are associated with a closed-open Syntaxin1 conformational transition. Here, we show that Syntaxin N-peptide binding to Munc18-1 is not highly selective, suggesting that other parts of the SNARE complex are involved in binding to Munc18-1. We also find that Syntaxin1, with an N peptide and a physically anchored C terminus, binds to Munc18-1 and that this complex can participate in SNARE complex formation. We report a Munc18-1-N-peptide crystal structure that, together with other data, reveals how Munc18-1 might transit from a conformation that binds closed Syntaxin1 to one that may be compatible with binding open Syntaxin1 and SNARE complexes. Our results suggest the possibility that structural transitions occur in both Munc18-1 and Syntaxin1 during their binary interaction. We hypothesize that Munc18-1 domain 3a undergoes a conformational change that may allow coiled-coil interactions with SNARE complexes. Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation.,Hu SH, Christie MP, Saez NJ, Latham CF, Jarrott R, Lua LH, Collins BM, Martin JL Proc Natl Acad Sci U S A. 2010 Dec 30. PMID:21193638[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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