3puj: Difference between revisions
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{{STRUCTURE_3puj| PDB=3puj | SCENE= }} | {{STRUCTURE_3puj| PDB=3puj | SCENE= }} | ||
===Crystal structure of the MUNC18-1 and SYNTAXIN4 N-Peptide complex=== | ===Crystal structure of the MUNC18-1 and SYNTAXIN4 N-Peptide complex=== | ||
{{ABSTRACT_PUBMED_21193638}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/STXB1_RAT STXB1_RAT]] May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions. [[http://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> | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <ref group="xtra">PMID:021193638</ref><references group="xtra"/><references/> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Christie, M P.]] | [[Category: Christie, M P.]] | ||
| Line 32: | Line 20: | ||
[[Category: Martin, J L.]] | [[Category: Martin, J L.]] | ||
[[Category: Saez, N J.]] | [[Category: Saez, N J.]] | ||
[[Category: Endocytosis-exocytosis complex]] | |||
[[Category: Membrane trafficking]] | |||
[[Category: Sm protein]] | |||
[[Category: Snare protein]] | |||
[[Category: Syntaxin]] | |||
[[Category: Syntaxin binding protein]] | |||
Revision as of 11:31, 8 May 2013
Crystal structure of the MUNC18-1 and SYNTAXIN4 N-Peptide complexCrystal structure of the MUNC18-1 and SYNTAXIN4 N-Peptide complex
Template:ABSTRACT PUBMED 21193638
FunctionFunction
[STXB1_RAT] May participate in the regulation of synaptic vesicle docking and fusion, possibly through interaction with GTP-binding proteins. Essential for neurotransmission and binds syntaxin, a component of the synaptic vesicle fusion machinery probably in a 1:1 ratio. Can interact with syntaxins 1, 2, and 3 but not syntaxin 4. May play a role in determining the specificity of intracellular fusion reactions. [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.[1] [2] [3]
About this StructureAbout this Structure
3puj is a 4 chain structure with sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Hu SH, Christie MP, Saez NJ, Latham CF, Jarrott R, Lua LH, Collins BM, Martin JL. Possible roles for Munc18-1 domain 3a and Syntaxin1 N-peptide and C-terminal anchor in SNARE complex formation. Proc Natl Acad Sci U S A. 2010 Dec 30. PMID:21193638 doi:10.1073/pnas.0914906108
- ↑ Tellam JT, Macaulay SL, McIntosh S, Hewish DR, Ward CW, James DE. Characterization of Munc-18c and syntaxin-4 in 3T3-L1 adipocytes. Putative role in insulin-dependent movement of GLUT-4. J Biol Chem. 1997 Mar 7;272(10):6179-86. PMID:9045631
- ↑ Min J, Okada S, Kanzaki M, Elmendorf JS, Coker KJ, Ceresa BP, Syu LJ, Noda Y, Saltiel AR, Pessin JE. Synip: a novel insulin-regulated syntaxin 4-binding protein mediating GLUT4 translocation in adipocytes. Mol Cell. 1999 Jun;3(6):751-60. PMID:10394363
- ↑ Pooley RD, Moynihan KL, Soukoulis V, Reddy S, Francis R, Lo C, Ma LJ, Bader DM. Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport. J Cell Sci. 2008 Oct 15;121(Pt 20):3413-21. doi: 10.1242/jcs.032847. Epub 2008, Sep 30. PMID:18827011 doi:10.1242/jcs.032847