1m2c

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[[Image:1m2c.jpg|left|200px]]
 
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==THREE-DIMENSIONAL STRUCTURE OF ALPHA-CONOTOXIN MII, NMR, 14 STRUCTURES==
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The line below this paragraph, containing "STRUCTURE_1m2c", creates the "Structure Box" on the page.
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<StructureSection load='1m2c' size='340' side='right'caption='[[1m2c]]' scene=''>
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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'>[[1m2c]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_magus Conus magus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M2C 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, 14 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_1m2c| PDB=1m2c | 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=1m2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2c OCA], [https://pdbe.org/1m2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m2c RCSB], [https://www.ebi.ac.uk/pdbsum/1m2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m2c ProSAT]</span></td></tr>
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</table>
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'''THREE-DIMENSIONAL STRUCTURE OF ALPHA-CONOTOXIN MII, NMR, 14 STRUCTURES'''
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== Function ==
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[https://www.uniprot.org/uniprot/CA12_CONMA CA12_CONMA] Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This toxin blocks neuronal mammalian nAChRs (alpha-6/alpha-3-beta-2-beta-3 (0.39 nM) > alpha-3-beta-2/CHRNA3-CHRNB2 > alpha-3-beta-4/CHRNA3-CHRNB4 = alpha-4-beta-2/CHRNA4-CHRNB2) (PubMed:15005608, PubMed:20145249). Also exhibits inhibition of D.melanogaster alpha-7/CHRNA7 nAChRs (PubMed:25466886). In addition, inhibits alpha-6/alpha-3-beta-4 (CHRNA6/CHRNA3-CHRNB4) nAChR with a higher potency on human (IC(50)=1.49 nM) than on rat receptors (IC(50)=31.5 nM) (PubMed:33523678). Its binding to alpha-3-beta-2/CHRNA3-CHRNB2 nAChR is prevented by alpha-conotoxin Lt1a, suggesting that the two toxins have overlapping binding sites (PubMed:20145249). In addition, both toxins have distinct nAChR binding mode (PubMed:20145249). In vivo, inhibits Ehrlich carcinoma growth and increase mouse survival (PubMed:32272633). These effects are greatly enhanced when the toxin is applied with the non-selective cyclooxygenase inhibitor indomethacin (PubMed:32272633).<ref>PMID:11044728</ref> <ref>PMID:15005608</ref> <ref>PMID:15044624</ref> <ref>PMID:15929983</ref> <ref>PMID:16964981</ref> <ref>PMID:20145249</ref> <ref>PMID:25466886</ref> <ref>PMID:32272633</ref> <ref>PMID:33523678</ref> <ref>PMID:8631783</ref>
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<div style="background-color:#fffaf0;">
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==Overview==
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== Publication Abstract from PubMed ==
We have isolated a 16-amino acid peptide from the venom of the marine snail Conus magus which potently blocks nicotinic acetylcholine receptors (nAChRs) composed of alpha3beta2 subunits. This peptide, named alpha-conotoxin MII, was identified by electrophysiologically screening venom fractions against cloned nicotinic receptors expressed in Xenopus oocytes. The peptide's structure, which has been confirmed by mass spectrometry and total chemical synthesis, differs significantly from those of all previously isolated alpha-conotoxins. Disulfide bridging, however, is conserved. The toxin blocks the response to acetylcholine in oocytes expressing alpha3beta2 nAChRs with an IC50 of 0.5 nM and is 2-4 orders of magnitude less potent on other nAChR subunit combinations. We have recently reported the isolation and characterization of alpha-conotoxin ImI, which selectively targets homomeric alpha7 neuronal nAChRs. Yet other alpha-conotoxins selectively block the muscle subtype of nAChR. Thus, it is increasingly apparent that alpha-conotoxins represent a significant resource for ligands with which to probe structure-function relationships of various nAChR subtypes.
We have isolated a 16-amino acid peptide from the venom of the marine snail Conus magus which potently blocks nicotinic acetylcholine receptors (nAChRs) composed of alpha3beta2 subunits. This peptide, named alpha-conotoxin MII, was identified by electrophysiologically screening venom fractions against cloned nicotinic receptors expressed in Xenopus oocytes. The peptide's structure, which has been confirmed by mass spectrometry and total chemical synthesis, differs significantly from those of all previously isolated alpha-conotoxins. Disulfide bridging, however, is conserved. The toxin blocks the response to acetylcholine in oocytes expressing alpha3beta2 nAChRs with an IC50 of 0.5 nM and is 2-4 orders of magnitude less potent on other nAChR subunit combinations. We have recently reported the isolation and characterization of alpha-conotoxin ImI, which selectively targets homomeric alpha7 neuronal nAChRs. Yet other alpha-conotoxins selectively block the muscle subtype of nAChR. Thus, it is increasingly apparent that alpha-conotoxins represent a significant resource for ligands with which to probe structure-function relationships of various nAChR subtypes.
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==About this Structure==
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A new alpha-conotoxin which targets alpha3beta2 nicotinic acetylcholine receptors.,Cartier GE, Yoshikami D, Gray WR, Luo S, Olivera BM, McIntosh JM J Biol Chem. 1996 Mar 29;271(13):7522-8. PMID:8631783<ref>PMID:8631783</ref>
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1M2C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Conus_magus Conus magus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2C OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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A new alpha-conotoxin which targets alpha3beta2 nicotinic acetylcholine receptors., Cartier GE, Yoshikami D, Gray WR, Luo S, Olivera BM, McIntosh JM, J Biol Chem. 1996 Mar 29;271(13):7522-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8631783 8631783]
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</div>
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<div class="pdbe-citations 1m2c" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Conus magus]]
[[Category: Conus magus]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Koerber, S C.]]
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[[Category: Koerber SC]]
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[[Category: Mcintosh, J M.]]
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[[Category: Mcintosh JM]]
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[[Category: Olivera, B M.]]
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[[Category: Olivera BM]]
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[[Category: Rivier, J E.]]
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[[Category: Rivier JE]]
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[[Category: Shon, K J.]]
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[[Category: Shon KJ]]
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[[Category: Cholinergic modulation]]
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[[Category: Dopamine release]]
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[[Category: Neuronal nicotinic acetylcholine receptor inhibitor]]
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[[Category: Neurotoxin]]
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[[Category: Presynaptic nicotinic acetylcholine receptor blocker]]
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[[Category: Subtype specific ligand]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:33:01 2008''
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THREE-DIMENSIONAL STRUCTURE OF ALPHA-CONOTOXIN MII, NMR, 14 STRUCTURES

PDB ID 1m2c

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