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1k64

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Revision as of 20:06, 24 December 2014

NMR Structue of alpha-conotoxin EI

Structural highlights

1k64 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	,
Related:	1plp, 1qs3, 1dg2
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[CXA1_CONER] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Blocks mammalian nAChR composed of alpha-1/gamma and alpha-1/delta subunits. Blocks central nervous system nAChR composed of alpha-4/beta-2 subunits and peripheral nervous system nAChR composed of alpha-3/beta-4 subunits. Low toxin concentrations potentiate currents in muscle nAChR composed of alpha-1/beta-1/gamma/delta subunits and central nervous system nAChR composed of alpha-4/beta-2 subunits, but not peripheral nervous system nAChR composed of alpha-3/beta-4 subunits.^[1] ^[2]

Publication Abstract from PubMed

A high resolution structure of alpha-conotoxin EI has been determined by (1)H NMR spectroscopy and molecular modeling. alpha-Conotoxin EI has the same disulfide framework as alpha 4/7 conotoxins targeting neuronal nicotinic acetylcholine receptors but antagonizes the neuromuscular receptor as do the alpha 3/5 and alpha A conotoxins. The unique binding preference of alpha-conotoxin EI to the alpha(1)/delta subunit interface of Torpedo neuromuscular receptor makes it a valuable structural template for superposition of various alpha-conotoxins possessing distinct receptor subtype specificities. Structural comparison of alpha-conotoxin EI with the gamma-subunit favoring alpha-conotoxin GI suggests that the Torpedo delta-subunit preference of the former originates from its second loop. Superposition of three-dimensional structures of seven alpha-conotoxins reveals that the estimated size of the toxin-binding pocket in nicotinic acetylcholine receptor is approximately 20 A (height) x 20 A (width) x 15 A (thickness).

Solution conformation of alpha-conotoxin EI, a neuromuscular toxin specific for the alpha 1/delta subunit interface of torpedo nicotinic acetylcholine receptor.,Park KH, Suk JE, Jacobsen R, Gray WR, McIntosh JM, Han KH J Biol Chem. 2001 Dec 28;276(52):49028-33. Epub 2001 Oct 18. PMID:11641403^[3]

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

References

↑ Martinez JS, Olivera BM, Gray WR, Craig AG, Groebe DR, Abramson SN, McIntosh JM. alpha-Conotoxin EI, a new nicotinic acetylcholine receptor antagonist with novel selectivity. Biochemistry. 1995 Nov 7;34(44):14519-26. PMID:7578057
↑ Lopez-Vera E, Aguilar MB, Schiavon E, Marinzi C, Ortiz E, Restano Cassulini R, Batista CV, Possani LD, Heimer de la Cotera EP, Peri F, Becerril B, Wanke E. Novel alpha-conotoxins from Conus spurius and the alpha-conotoxin EI share high-affinity potentiation and low-affinity inhibition of nicotinic acetylcholine receptors. FEBS J. 2007 Aug;274(15):3972-85. Epub 2007 Jul 16. PMID:17635581 doi:http://dx.doi.org/10.1111/j.1742-4658.2007.05931.x
↑ Park KH, Suk JE, Jacobsen R, Gray WR, McIntosh JM, Han KH. Solution conformation of alpha-conotoxin EI, a neuromuscular toxin specific for the alpha 1/delta subunit interface of torpedo nicotinic acetylcholine receptor. J Biol Chem. 2001 Dec 28;276(52):49028-33. Epub 2001 Oct 18. PMID:11641403 doi:10.1074/jbc.M107798200

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/1k64"

@@ Line 7: / Line 7: @@
 <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=1k64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k64 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k64 RCSB], [http://www.ebi.ac.uk/pdbsum/1k64 PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CXA1_CONER CXA1_CONER]] Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them. Blocks mammalian nAChR composed of alpha-1/gamma and alpha-1/delta subunits. Blocks central nervous system nAChR composed of alpha-4/beta-2 subunits and peripheral nervous system nAChR composed of alpha-3/beta-4 subunits. Low toxin concentrations potentiate currents in muscle nAChR composed of alpha-1/beta-1/gamma/delta subunits and central nervous system nAChR composed of alpha-4/beta-2 subunits, but not peripheral nervous system nAChR composed of alpha-3/beta-4 subunits.<ref>PMID:7578057</ref> <ref>PMID:17635581</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

1k64

From Proteopedia

Revision as of 20:06, 24 December 2014

NMR Structue of alpha-conotoxin EI

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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