Nmr Structure Determination of Alpha-conotoxin Buia, a Novel Neuronal Nicotinic Acetylcholine Receptor Antagonist with an Unusual 4/4 Disulfide Scaffold.
From: Molecular Cancer Research Center, Division of Molecular Therapeutics, KRIBB, Daejeon 305-806, Republic of Korea.
Biochemical and biophysical research communications
- Publish Date: Nov 2006
- ISSN: 0006-291X
- Volume: 349
- Issue: 4
- Pages: 1228-34
- Medium: Print
- Language: English
- Citation (JAMA): Chi Seung-Wook, Kim Do-Hyoung, Olivera Baldomero M, et al. Nmr Structure Determination of Alpha-conotoxin Buia, a Novel Neuronal Nicotinic Acetylcholine Receptor Antagonist with an Unusual 4/4 Disulfide Scaffold.. Biochem. Biophys. Res. Commun. Nov 2006;349:1228-34
Abstract
We have determined a high-resolution three-dimensional structure of alpha-conotoxin BuIA, a 13-residue peptide toxin isolated from Conus bullatus. Despite its unusual 4/4 disulfide bond layout alpha-conotoxin BuIA exhibits strong antagonistic activity at alpha6/alpha3beta2beta3, alpha3beta2, and alpha3beta4 nAChR subtypes like some alpha4/7 conotoxins. alpha-Conotoxin BuIA lacks the C-terminal beta-turn present within the second disulfide loop of alpha4/7 conotoxins, having only a “pseudo omega-shaped” molecular topology. Nevertheless, it contains a functionally critical two-turn helix motif, a feature ubiquitously found in alpha4/7 conotoxins. Such an aspect seems mainly responsible for similarities in the receptor recognition profile of alpha-conotoxin BuIA to alpha4/7 conotoxins. Structural comparison of alpha-conotoxin BuIA with alpha4/7 conotoxins and alpha4/3 conotoxin ImI suggests that presence of the second helical turn portion of the two-turn helix motif in alpha4/7 and alpha4/4 conotoxins may be important for binding to the alpha3 and/or alpha6 subunit of nAChR.
Mesh Headings (Keywords): Animals, Binding Sites, Computer Simulation, Conotoxins, Conus Snail, Crystallography, Disulfides, Magnetic Resonance Spectroscopy, Models, Chemical, Models, Molecular, Molecular Conformation, Nicotinic Antagonists, Protein Binding, Receptors, Nicotinic
Check for Full Text / PubMed Unique Identifier (PMID): 16979596
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