2bc7

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{{Seed}}
 
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[[Image:2bc7.png|left|200px]]
 
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==Solution structure of [Sec2,8]-ImI==
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The line below this paragraph, containing "STRUCTURE_2bc7", creates the "Structure Box" on the page.
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<StructureSection load='2bc7' size='340' side='right'caption='[[2bc7]]' 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'>[[2bc7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_imperialis Conus imperialis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BC7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BC7 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, 20 models</td></tr>
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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=2bc7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bc7 OCA], [https://pdbe.org/2bc7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bc7 RCSB], [https://www.ebi.ac.uk/pdbsum/2bc7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bc7 ProSAT]</span></td></tr>
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{{STRUCTURE_2bc7| PDB=2bc7 | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CA1_CONIM CA1_CONIM] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks mammalian neuronal nAChRs (alpha-3/beta-2 > alpha-7 > alpha-3/beta-4). Has no effect on nAChRs composed of alpha-2/beta-2, alpha-3/beta-2, alpha-4/beta-2, alpha-2/beta-4, alpha-3/beta-4, or alpha-4/beta-4 subunits. Acts voltage-independently. Is highly active against the neuromuscular receptor in frog.<ref>PMID:8206995</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Disulfide bonds are important structural motifs that play an essential role in maintaining the conformational stability of many bioactive peptides. Of particular importance are the conotoxins, which selectively target a wide range of ion channels that are implicated in numerous disease states. Despite the enormous potential of conotoxins as therapeutics, their multiple disulfide bond frameworks are inherently unstable under reducing conditions. Reduction or scrambling by thiol-containing molecules such as glutathione or serum albumin in intracellular or extracellular environments such as blood plasma can decrease their effectiveness as drugs. To address this issue, we describe a new class of selenoconotoxins where cysteine residues are replaced by selenocysteine to form isosteric and nonreducible diselenide bonds. Three isoforms of alpha-conotoxin ImI were synthesized by t-butoxycarbonyl chemistry with systematic replacement of one ([Sec(2,8)]ImI or [Sec(3,12)]ImI), or both ([Sec(2,3,8,12)]ImI) disulfide bonds with a diselenide bond. Each analogue demonstrated remarkable stability to reduction or scrambling under a range of chemical and biological reducing conditions. Three-dimensional structural characterization by NMR and CD spectroscopy indicates conformational preferences that are very similar to those of native ImI, suggesting fully isomorphic structures. Additionally, full bioactivity was retained at the alpha7 nicotinic acetylcholine receptor, with each selenoanalogue exhibiting a dose-response curve that overlaps with wild-type ImI, thus further supporting an isomorphic structure. These results demonstrate that selenoconotoxins can be used as highly stable scaffolds for the design of new drugs.
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===Solution structure of [Sec2,8]-ImI===
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Alpha-selenoconotoxins, a new class of potent alpha7 neuronal nicotinic receptor antagonists.,Armishaw CJ, Daly NL, Nevin ST, Adams DJ, Craik DJ, Alewood PF J Biol Chem. 2006 May 19;281(20):14136-43. Epub 2006 Feb 24. PMID:16500898<ref>PMID:16500898</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 class="pdbe-citations 2bc7" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 16500898 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16500898}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Conus imperialis]]
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2BC7 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BC7 OCA].
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[[Category: Large Structures]]
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[[Category: Armishaw CJ]]
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==Reference==
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Alpha-selenoconotoxins, a new class of potent alpha7 neuronal nicotinic receptor antagonists., Armishaw CJ, Daly NL, Nevin ST, Adams DJ, Craik DJ, Alewood PF, J Biol Chem. 2006 May 19;281(20):14136-43. Epub 2006 Feb 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16500898 16500898]
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[[Category: Single protein]]
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[[Category: Armishaw, C J.]]
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[[Category: Diselenide bond]]
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[[Category: Disulfide bond]]
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[[Category: Helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 13:12:39 2008''
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Current revision

Solution structure of [Sec2,8]-ImI

PDB ID 2bc7

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