Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 281, Issue 34, Pages 24678-24686Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M602969200
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Funding
- NIDA NIH HHS [U01 DA019372, U01-DA019372] Funding Source: Medline
- NIGMS NIH HHS [GM48677, R37-GM18360, P01 GM048677, R37 GM018360] Funding Source: Medline
- NIMH NIH HHS [R01 MH053631-11S1, R01 MH053631, R01 MH053631-11, MH53631, R29 MH053631] Funding Source: Medline
- NINDS NIH HHS [NS 043063, F32 NS043063-01, F32 NS043063] Funding Source: Medline
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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 alpha-subunit of nicotinic acetylcholine receptors and in particular the homomeric alpha 7 nicotinic receptor. We report the isolation and characterization of an alpha-conotoxin that has the highest known affinity for the Lymnaea AChBP and also potently blocks the alpha 7 nAChR subtype when expressed in Xenopus oocytes. Remarkably, the peptide also has high affinity for the alpha 3 beta 2 nAChR indicating that alpha-conotoxin OmIA in combination with the AChBP may serve as a model system for understanding the binding determinants of alpha 3 beta 2 nAChRs. alpha-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 alpha-conotoxin with higher affinity for the closely related receptor subtypes, alpha 3 beta 2 versus alpha 6 beta 2, and selectively blocks these two subtypes when compared with alpha 2 beta 2, alpha 4 beta 2, and alpha 1 beta 1 delta epsilon nAChRs.
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