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1mxn

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(New page: 200px<br /><applet load="1mxn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mxn" /> '''Solution structure of alpha-conotoxin AuIB''...)
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[[Image:1mxn.gif|left|200px]]<br /><applet load="1mxn" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1mxn" />
 
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'''Solution structure of alpha-conotoxin AuIB'''<br />
 
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==Overview==
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==Solution structure of alpha-conotoxin AuIB==
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alpha-Conotoxin AuIB and a disulfide bond variant of AuIB have been, synthesized to determine the role of disulfide bond connectivity on, structure and activity. Both of these peptides contain the 15 amino acid, sequence GCCSYPPCFATNPDC, with the globular (native) isomer having the, disulfide connectivity Cys(2-8 and 3-15) and the ribbon isomer having the, disulfide connectivity Cys(2-15 and 3-8). The solution structures of the, peptides were determined by NMR spectroscopy, and their ability to block, the nicotinic acetylcholine receptors on dissociated neurons of the rat, parasympathetic ganglia was examined. The ribbon disulfide isomer, although having a less well defined structure, is surprisingly found to, have approximately 10 times greater potency than the native peptide. To, our knowledge this is the first demonstration of a non-native disulfide, bond isomer of a conotoxin exhibiting greater biological activity than the, native isomer.
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<StructureSection load='1mxn' size='340' side='right'caption='[[1mxn]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1mxn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_aulicus Conus aulicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MXN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MXN 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</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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mxn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mxn OCA], [https://pdbe.org/1mxn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mxn RCSB], [https://www.ebi.ac.uk/pdbsum/1mxn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mxn ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/CA1B_CONAL CA1B_CONAL] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin blocks mammalian nAChR alpha-3/beta-4 subunits.<ref>PMID:9786965</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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alpha-Conotoxin AuIB and a disulfide bond variant of AuIB have been synthesized to determine the role of disulfide bond connectivity on structure and activity. Both of these peptides contain the 15 amino acid sequence GCCSYPPCFATNPDC, with the globular (native) isomer having the disulfide connectivity Cys(2-8 and 3-15) and the ribbon isomer having the disulfide connectivity Cys(2-15 and 3-8). The solution structures of the peptides were determined by NMR spectroscopy, and their ability to block the nicotinic acetylcholine receptors on dissociated neurons of the rat parasympathetic ganglia was examined. The ribbon disulfide isomer, although having a less well defined structure, is surprisingly found to have approximately 10 times greater potency than the native peptide. To our knowledge this is the first demonstration of a non-native disulfide bond isomer of a conotoxin exhibiting greater biological activity than the native isomer.
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==About this Structure==
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A new level of conotoxin diversity, a non-native disulfide bond connectivity in alpha-conotoxin AuIB reduces structural definition but increases biological activity.,Dutton JL, Bansal PS, Hogg RC, Adams DJ, Alewood PF, Craik DJ J Biol Chem. 2002 Dec 13;277(50):48849-57. Epub 2002 Oct 9. PMID:12376538<ref>PMID:12376538</ref>
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1MXN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MXN 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 level of conotoxin diversity, a non-native disulfide bond connectivity in alpha-conotoxin AuIB reduces structural definition but increases biological activity., Dutton JL, Bansal PS, Hogg RC, Adams DJ, Alewood PF, Craik DJ, J Biol Chem. 2002 Dec 13;277(50):48849-57. Epub 2002 Oct 9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12376538 12376538]
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</div>
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[[Category: Single protein]]
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<div class="pdbe-citations 1mxn" style="background-color:#fffaf0;"></div>
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[[Category: Adams, D.J.]]
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== References ==
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[[Category: Alewood, P.F.]]
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<references/>
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[[Category: Bansal, P.S.]]
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__TOC__
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[[Category: Craik, D.J.]]
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</StructureSection>
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[[Category: Dutton, J.L.]]
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[[Category: Conus aulicus]]
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[[Category: Hogg, R.C.]]
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[[Category: Large Structures]]
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[[Category: NH2]]
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[[Category: Adams DJ]]
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[[Category: alpha helix]]
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[[Category: Alewood PF]]
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[[Category: Bansal PS]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:47:04 2007''
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[[Category: Craik DJ]]
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[[Category: Dutton JL]]
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[[Category: Hogg RC]]

Current revision

Solution structure of alpha-conotoxin AuIB

PDB ID 1mxn

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