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2ns3
From Proteopedia
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| - | [[Image:2ns3.jpg|left|200px]] | ||
| - | + | ==Solution structure of ribbon BuIA== | |
| - | + | <StructureSection load='2ns3' size='340' side='right'caption='[[2ns3]]' scene=''> | |
| - | | | + | == Structural highlights == |
| - | | | + | <table><tr><td colspan='2'>[[2ns3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conus_bullatus Conus bullatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2NS3 FirstGlance]. <br> |
| - | + | </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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=2ns3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ns3 OCA], [https://pdbe.org/2ns3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ns3 RCSB], [https://www.ebi.ac.uk/pdbsum/2ns3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ns3 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | + | == Function == | |
| - | + | [https://www.uniprot.org/uniprot/CA1A_CONBU CA1A_CONBU] Alpha-conotoxins bind to the nicotinic acetylcholine receptors (nAChR) and inhibit them. This peptide potently blocks numerous mammalian nAChR subtypes (alpha-6 or -3/beta-2 or -3 > alpha-6 or-3/beta-4 > alpha-3/beta-2 > alpha-3/beta-4 > alpha-4/beta-4 = alpha-2/beta-4 > alpha-7 > alpha-2/beta-2 >> alpha-4/beta-2). Recovery from toxin block is markedly slower for beta-4 versus beta-2 subunit-containing nAChRs. Thus, it represents a novel probe for distinguishing between beta-2 and beta-4-containing nAChRs. | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | + | == Publication Abstract from PubMed == | |
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BACKGROUND: Alpha-conotoxins have exciting therapeutic potential based on their high selectivity and affinity for nicotinic acetylcholine receptors. The spacing between the cysteine residues in alpha-conotoxins is variable, leading to the classification of sub-families. BuIA is the only alpha-conotoxin containing a 4/4 cysteine spacing and thus it is of significant interest to examine the structure of this conotoxin. RESULTS: In the current study we show the native globular disulfide connectivity of BuIA displays multiple conformations in solution whereas the non-native ribbon isomer has a single well-defined conformation. Despite having multiple conformations in solution the globular form of BuIA displays activity at the nicotinic acetylcholine receptor, contrasting with the lack of activity of the structurally well-defined ribbon isomer. CONCLUSION: These findings are opposite to the general trends observed for alpha-conotoxins where the native isomers have well-defined structures and the ribbon isomers are generally disordered. This study thus highlights the influence of the disulfide connectivity of BuIA on the dynamics of the three-dimensional structure. | BACKGROUND: Alpha-conotoxins have exciting therapeutic potential based on their high selectivity and affinity for nicotinic acetylcholine receptors. The spacing between the cysteine residues in alpha-conotoxins is variable, leading to the classification of sub-families. BuIA is the only alpha-conotoxin containing a 4/4 cysteine spacing and thus it is of significant interest to examine the structure of this conotoxin. RESULTS: In the current study we show the native globular disulfide connectivity of BuIA displays multiple conformations in solution whereas the non-native ribbon isomer has a single well-defined conformation. Despite having multiple conformations in solution the globular form of BuIA displays activity at the nicotinic acetylcholine receptor, contrasting with the lack of activity of the structurally well-defined ribbon isomer. CONCLUSION: These findings are opposite to the general trends observed for alpha-conotoxins where the native isomers have well-defined structures and the ribbon isomers are generally disordered. This study thus highlights the influence of the disulfide connectivity of BuIA on the dynamics of the three-dimensional structure. | ||
| - | + | Structure of alpha-conotoxin BuIA: influences of disulfide connectivity on structural dynamics.,Jin AH, Brandstaetter H, Nevin ST, Tan CC, Clark RJ, Adams DJ, Alewood PF, Craik DJ, Daly NL BMC Struct Biol. 2007 Apr 20;7:28. PMID:17445276<ref>PMID:17445276</ref> | |
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| - | Structure of alpha-conotoxin BuIA: influences of disulfide connectivity on structural dynamics., Jin AH, Brandstaetter H, Nevin ST, Tan CC, Clark RJ, Adams DJ, Alewood PF, Craik DJ, Daly NL | + | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 2ns3" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Conus bullatus]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Adams DJ]] | ||
| + | [[Category: Alewood PF]] | ||
| + | [[Category: Brandstaetter H]] | ||
| + | [[Category: Clark RJ]] | ||
| + | [[Category: Craik DJ]] | ||
| + | [[Category: Daly NL]] | ||
| + | [[Category: Jin AH]] | ||
| + | [[Category: Nevin ST]] | ||
| + | [[Category: Tan CC]] | ||
Current revision
Solution structure of ribbon BuIA
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Categories: Conus bullatus | Large Structures | Adams DJ | Alewood PF | Brandstaetter H | Clark RJ | Craik DJ | Daly NL | Jin AH | Nevin ST | Tan CC
