This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1mxp

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB

Structural highlights

1mxp is a 1 chain structure with sequence from Conus aulicus. 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

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.^[1]

Publication Abstract from PubMed

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.

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^[2]

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

References

↑ Luo S, Kulak JM, Cartier GE, Jacobsen RB, Yoshikami D, Olivera BM, McIntosh JM. alpha-conotoxin AuIB selectively blocks alpha3 beta4 nicotinic acetylcholine receptors and nicotine-evoked norepinephrine release. J Neurosci. 1998 Nov 1;18(21):8571-9. PMID:9786965
↑ Dutton JL, Bansal PS, Hogg RC, Adams DJ, Alewood PF, Craik DJ. A new level of conotoxin diversity, a non-native disulfide bond connectivity in alpha-conotoxin AuIB reduces structural definition but increases biological activity. J Biol Chem. 2002 Dec 13;277(50):48849-57. Epub 2002 Oct 9. PMID:12376538 doi:10.1074/jbc.M208842200

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/1mxp"

@@ Line 1: / Line 1: @@
 ==Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB==
-<StructureSection load='1mxp' size='340' side='right' caption='[[1mxp]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1mxp' size='340' side='right'caption='[[1mxp]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1mxp]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MXP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1MXP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1mxp]] 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=1MXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MXP 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mxn|1mxn]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mxp OCA], [http://pdbe.org/1mxp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1mxp RCSB], [http://www.ebi.ac.uk/pdbsum/1mxp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1mxp ProSAT]</span></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=1mxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mxp OCA], [https://pdbe.org/1mxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mxp RCSB], [https://www.ebi.ac.uk/pdbsum/1mxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mxp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 23: / Line 23: @@
 __TOC__
 </StructureSection>
-[[Category: Adams, D J]]
+[[Category: Conus aulicus]]
-[[Category: Alewood, P F]]
+[[Category: Large Structures]]
-[[Category: Bansal, P S]]
+[[Category: Adams DJ]]
-[[Category: Craik, D J]]
+[[Category: Alewood PF]]
-[[Category: Dutton, J L]]
+[[Category: Bansal PS]]
-[[Category: Hogg, R C]]
+[[Category: Craik DJ]]
-[[Category: Toxin]]
+[[Category: Dutton JL]]
-[[Category: Turn]]
+[[Category: Hogg RC]]

1mxp

From Proteopedia

Current revision

Solution structure of the ribbon disulfide bond isomer of alpha-conotoxin AuIB

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox