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Title 

α-conotoxin OmIA is a potent ligand for the acetylcholine-binding protein as well as α3β2 and α7 nicotinic acetylcholine receptors

Authors 

T T TalleyB M OliveraKyou Hoon HanS B ChristensenC DowellI TsigelnyK Y HoP TaylorJ M McIntosh

Publisher 

American Society for Biochemistry and Molecular Biology

Issue Date 

2006

Citation 

Journal of Biological Chemistry, vol. 281, no. 34, pp. 24678-24686

Keywords 

amino acidschemical bondsextracellular bindingnicotinic acetylcholineproteinsacetylcholineacetylcholine binding proteinbinding proteinbungarotoxin receptorcholinergic receptor

Abstract 

The molluskan acetylcholine-binding protein (AChBP) is a homolog of the extracellular binding domain of the pentameric ligand-gated ion channel family. AChBP most closely resembles the α-subunit of nicotinic acetylcholine receptors and in particular the homomeric α7 nicotinic receptor. We report the isolation and characterization of an α-conotoxin that has the highest known affinity for the Lymnaea AChBP and also potently blocks the α7 nAChR subtype when expressed in Xenopus oocytes. Remarkably, the peptide also has high affinity for the α3β2 nAChR indicating that α-conotoxin OmIA in combination with the AChBP may serve as a model system for understanding the binding determinants of α3β2 nAChRs. α-Conotoxin OmIA was purified from the venom of Conus omaria. It is a 17-amino-acid, two-disulfide bridge peptide. The ligand is the first α-conotoxin with higher affinity for the closely related receptor subtypes, α3β2 versus α6β2, and selectively blocks these two subtypes when compared with α2β2, α4β2, and α1β1δε nAChRs.

ISSN 

0021-9258

Link 

http://dx.doi.org/10.1074/jbc.M602969200

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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