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| | ==Solution Conformation of alphaA-Conotoxin EIVA== | | ==Solution Conformation of alphaA-Conotoxin EIVA== |
| - | <StructureSection load='1pqr' size='340' side='right' caption='[[1pqr]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''> | + | <StructureSection load='1pqr' size='340' side='right'caption='[[1pqr]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1pqr]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PQR FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1pqr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_ermineus Conus ermineus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PQR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PQR FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pqr OCA], [http://pdbe.org/1pqr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pqr RCSB], [http://www.ebi.ac.uk/pdbsum/1pqr PDBsum]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1pqr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pqr OCA], [https://pdbe.org/1pqr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pqr RCSB], [https://www.ebi.ac.uk/pdbsum/1pqr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pqr ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CA4A_CONER CA4A_CONER]] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin binds with high affinity to both fetal (alpha-1/beta-1/epsilon/delta subunits) and adult (alpha-1/beta-1/gamma/delta subunits) mammalian muscle nicotinic acetylcholine receptors (nAChR). | + | [https://www.uniprot.org/uniprot/CA4A_CONER CA4A_CONER] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin binds with high affinity to both fetal (alpha-1/beta-1/epsilon/delta subunits) and adult (alpha-1/beta-1/gamma/delta subunits) mammalian muscle nicotinic acetylcholine receptors (nAChR). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chi, S W]] | + | [[Category: Conus ermineus]] |
| - | [[Category: Han, K H]] | + | [[Category: Large Structures]] |
| - | [[Category: McIntosh, J M]] | + | [[Category: Chi S-W]] |
| - | [[Category: Olivera, B M]] | + | [[Category: Han K-H]] |
| - | [[Category: Park, K H]]
| + | [[Category: McIntosh JM]] |
| - | [[Category: Suk, J E]] | + | [[Category: Olivera BM]] |
| - | [[Category: Alpha-helix]] | + | [[Category: Park K-H]] |
| - | [[Category: C-term amidation]] | + | [[Category: Suk J-E]] |
| - | [[Category: Toxin]] | + | |
| - | [[Category: Two disulfide bond]]
| + | |
| Structural highlights
Function
CA4A_CONER Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. This toxin binds with high affinity to both fetal (alpha-1/beta-1/epsilon/delta subunits) and adult (alpha-1/beta-1/gamma/delta subunits) mammalian muscle nicotinic acetylcholine receptors (nAChR).
Publication Abstract from PubMed
We report the solution three-dimensional structure of an alphaA-conotoxin EIVA determined by nuclear magnetic resonance spectroscopy and restrained molecular dynamics. The alphaA-conotoxin EIVA consists of 30 amino acids representing the largest peptide among the alpha/alphaA-family conotoxins discovered so far and targets the neuromuscular nicotinic acetylcholine receptor with high affinity. alphaA-Conotoxin EIVA consists of three distinct structural domains. The first domain is mainly composed of the Cys3-Cys11-disulfide loop and is structurally ill-defined with a large backbone root mean square deviation of 1.91 A. The second domain formed by residues His12-Hyp21 is extremely well defined with a backbone root mean square deviation of 0.52 A, thus forming a sturdy stem for the entire molecule. The third C-terminal domain formed by residues Hyp22-Gly29 shows an intermediate structural order having a backbone root mean square deviation of 1.04 A. A structurally ill-defined N-terminal first loop domain connected to a rigid central molecular stem seems to be the general structural feature of the alphaA-conotoxin subfamily. A detailed structural comparison between alphaA-conotoxin EIVA and alphaA-conotoxin PIVA suggests that the higher receptor affinity of alphaA-conotoxin EIVA than alphaA-conotoxin PIVA might originate from different steric disposition and charge distribution in the second loop "handle" motif.
Solution conformation of alphaA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus.,Chi SW, Park KH, Suk JE, Olivera BM, McIntosh JM, Han KH J Biol Chem. 2003 Oct 24;278(43):42208-13. Epub 2003 Aug 4. PMID:12900418[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chi SW, Park KH, Suk JE, Olivera BM, McIntosh JM, Han KH. Solution conformation of alphaA-conotoxin EIVA, a potent neuromuscular nicotinic acetylcholine receptor antagonist from Conus ermineus. J Biol Chem. 2003 Oct 24;278(43):42208-13. Epub 2003 Aug 4. PMID:12900418 doi:http://dx.doi.org/10.1074/jbc.M303342200
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