1qmw

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{{Seed}}
 
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[[Image:1qmw.png|left|200px]]
 
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==Solution structure of alpha-conotoxin SI==
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The line below this paragraph, containing "STRUCTURE_1qmw", creates the "Structure Box" on the page.
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<StructureSection load='1qmw' size='340' side='right'caption='[[1qmw]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[1qmw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_striatus Conus striatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QMW FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 36 models</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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{{STRUCTURE_1qmw| PDB=1qmw | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qmw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmw OCA], [https://pdbe.org/1qmw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qmw RCSB], [https://www.ebi.ac.uk/pdbsum/1qmw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qmw ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CA1_CONST CA1_CONST] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them (PubMed:3196703). Is active on muscle nAChR (IC(50)=113 nM on adult subtype (alpha-1-beta-1-gamma-delta/CHRNA1-CHRNB1-CHRNG-CHRND) and IC(50)=142 nM on fetal subtype (alpha-1-beta-1-delta-epsilon/CHRNA1-CHRNB1-CHRND-CHRNE)) (PubMed:35357806, PubMed:9174364). On mice muscle receptors, its higher affinity site is the alpha/delta nAChR subunit interface (PubMed:9174364). On Torpedo receptors, it does not distinguish between alpha/delta and alpha/gamma acetylcholine-binding sites (PubMed:9174364). In vivo, causes paralysis followed by death when injected into goldfish (PubMed:3196703). In contrast, has no effect on mice, when similar doses are intraperitoneally or intracerebrally injected (PubMed:3196703).<ref>PMID:3196703</ref> <ref>PMID:35357806</ref> <ref>PMID:9174364</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The nuclear magnetic resonance solution structure of alpha-conotoxin SI has been determined at pH 4.2. The 36 lowest energy structures show that alpha-conotoxin SI exists in a single major solution conformation and is stabilized by six hydrogen bonds. Comparisons are made between the SI solution structure and the solution and crystal structures of alpha-conotoxin GI. Surprisingly, a high degree of similarity between the backbone conformations of the GI crystal and the SI solution structures is seen in the region of lowest sequence homology, namely residues Gly-8 to Ser-12. This similarity is more surprising when considering that in SI a proline replaces the Arg-9 found in GI. The correspondence in conformation in this region provides the definitive evidence that it is the loss of the arginine basic charge at residue 9 which determines the differences in toxicity between GI and SI, rather than any changes in conformation induced by the cyclic proline residue.
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===SOLUTION STRUCTURE OF ALPHA-CONOTOXIN SI===
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Solution structure of alpha-conotoxin SI.,Benie AJ, Whitford D, Hargittai B, Barany G, Janes RW FEBS Lett. 2000 Jul 7;476(3):287-95. PMID:10913630<ref>PMID:10913630</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_10913630}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1qmw" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 10913630 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_10913630}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1QMW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Conus_striatus Conus striatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMW OCA].
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==Reference==
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Solution structure of alpha-conotoxin SI., Benie AJ, Whitford D, Hargittai B, Barany G, Janes RW, FEBS Lett. 2000 Jul 7;476(3):287-95. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10913630 10913630]
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[[Category: Conus striatus]]
[[Category: Conus striatus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Barany, G.]]
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[[Category: Barany G]]
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[[Category: Benie, A J.]]
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[[Category: Benie AJ]]
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[[Category: Hargittai, B.]]
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[[Category: Hargittai B]]
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[[Category: Janes, R W.]]
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[[Category: Janes RW]]
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[[Category: Whitford, D.]]
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[[Category: Whitford D]]
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[[Category: Conotoxin]]
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[[Category: Nicotinic acetylcholine receptor]]
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[[Category: Toxin]]
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[[Category: Venom]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:25:54 2008''
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Current revision

Solution structure of alpha-conotoxin SI

PDB ID 1qmw

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