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2ns3

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Solution structure of ribbon BuIA

Structural highlights

2ns3 is a 1 chain structure with sequence from Conus bullatus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.

Publication Abstract from PubMed

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jin AH, Brandstaetter H, Nevin ST, Tan CC, Clark RJ, Adams DJ, Alewood PF, Craik DJ, Daly NL. Structure of alpha-conotoxin BuIA: influences of disulfide connectivity on structural dynamics. BMC Struct Biol. 2007 Apr 20;7:28. PMID:17445276 doi:http://dx.doi.org/1472-6807-7-28

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ns3"

@@ Line 1: / Line 1: @@
 ==Solution structure of ribbon BuIA==
-<StructureSection load='2ns3' size='340' side='right'caption='[[2ns3]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2ns3' size='340' side='right'caption='[[2ns3]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ns3]] is a 1 chain structure. 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 [http://proteopedia.org/fgij/fg.htm?mol=2NS3 FirstGlance]. <br>
+<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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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://proteopedia.org/fgij/fg.htm?mol=2ns3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ns3 OCA], [http://pdbe.org/2ns3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ns3 RCSB], [http://www.ebi.ac.uk/pdbsum/2ns3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ns3 ProSAT]</span></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 ==
-[[http://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.
+[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 ==
@@ Line 22: / Line 23: @@
 __TOC__
 </StructureSection>
+[[Category: Conus bullatus]]
 [[Category: Large Structures]]
-[[Category: Adams, D J]]
+[[Category: Adams DJ]]
-[[Category: Alewood, P F]]
+[[Category: Alewood PF]]
-[[Category: Brandstaetter, H]]
+[[Category: Brandstaetter H]]
-[[Category: Clark, R J]]
+[[Category: Clark RJ]]
-[[Category: Craik, D J]]
+[[Category: Craik DJ]]
-[[Category: Daly, N L]]
+[[Category: Daly NL]]
-[[Category: Jin, A H]]
+[[Category: Jin AH]]
-[[Category: Nevin, S T]]
+[[Category: Nevin ST]]
-[[Category: Tan, C C]]
+[[Category: Tan CC]]
-[[Category: Ribbon disulfide connectivity]]
-[[Category: Toxin]]

2ns3

From Proteopedia

Current revision

Solution structure of ribbon BuIA

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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