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< | ==THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A== | ||
<StructureSection load='1br0' size='340' side='right'caption='[[1br0]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1br0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. The November 2013 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''SNARE Proteins'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2013_11 10.2210/rcsb_pdb/mom_2013_11]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BR0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BR0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1br0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1br0 OCA], [https://pdbe.org/1br0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1br0 RCSB], [https://www.ebi.ac.uk/pdbsum/1br0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1br0 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/br/1br0_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1br0 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Syntaxin 1A plays a central role in neurotransmitter release through multiple protein-protein interactions. We have used NMR spectroscopy to identify an autonomously folded N-terminal domain in syntaxin 1A and to elucidate its three-dimensional structure. This 120-residue N-terminal domain is conserved in plasma membrane syntaxins but not in other syntaxins, indicating a specific role in exocytosis. The domain contains three long alpha helices that form an up-and-down bundle with a left-handed twist. A striking residue conservation is observed throughout a long groove that is likely to provide a specific surface for protein-protein interactions. A highly acidic region binds to the C2A domain of synaptotagmin I in a Ca2+-dependent interaction that may serve as an electrostatic switch in neurotransmitter release. | |||
Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A.,Fernandez I, Ubach J, Dulubova I, Zhang X, Sudhof TC, Rizo J Cell. 1998 Sep 18;94(6):841-9. PMID:9753330<ref>PMID:9753330</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1br0" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Syntaxin 3D structures|Syntaxin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: RCSB PDB Molecule of the Month]] | |||
== | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: | [[Category: SNARE Proteins]] | ||
[[Category: Dubulova | [[Category: Dubulova I]] | ||
[[Category: Fernandez | [[Category: Fernandez I]] | ||
[[Category: Rizo | [[Category: Rizo J]] | ||
[[Category: Sudhof | [[Category: Sudhof TC]] | ||
[[Category: Ubach | [[Category: Ubach J]] | ||
[[Category: Zhang | [[Category: Zhang X]] | ||
Latest revision as of 11:19, 22 May 2024
THREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1ATHREE DIMENSIONAL STRUCTURE OF THE N-TERMINAL DOMAIN OF SYNTAXIN 1A
Structural highlights
FunctionSTX1A_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 PubMedSyntaxin 1A plays a central role in neurotransmitter release through multiple protein-protein interactions. We have used NMR spectroscopy to identify an autonomously folded N-terminal domain in syntaxin 1A and to elucidate its three-dimensional structure. This 120-residue N-terminal domain is conserved in plasma membrane syntaxins but not in other syntaxins, indicating a specific role in exocytosis. The domain contains three long alpha helices that form an up-and-down bundle with a left-handed twist. A striking residue conservation is observed throughout a long groove that is likely to provide a specific surface for protein-protein interactions. A highly acidic region binds to the C2A domain of synaptotagmin I in a Ca2+-dependent interaction that may serve as an electrostatic switch in neurotransmitter release. Three-dimensional structure of an evolutionarily conserved N-terminal domain of syntaxin 1A.,Fernandez I, Ubach J, Dulubova I, Zhang X, Sudhof TC, Rizo J Cell. 1998 Sep 18;94(6):841-9. PMID:9753330[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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