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  • Three-dimensional structure of the a-conotoxin GI at 1.2 Å resolution

    Author(s)
    Guddat, LW
    Martin, JL
    Shan, L
    Edmundson, AB
    Gray, WR
    Griffith University Author(s)
    Martin, Jennifer
    Year published
    1996
    Metadata
    Show full item record
    Abstract
    Predatory marine snails of the genus Conus paralyze their fish prey by injecting a potent toxin. The α-conotoxin GI is a 13-residue peptide isolated from venom of Conus geographus. It functions by blocking the postsynaptic nicotinic acetylcholine receptor. After crystallization in deionized water, the three-dimensional structure of the GI neurotoxin was determined to 1.2 Å resolution by X-ray crystallography. This structure, which can be described as a trianglar slab, shows overall similarities to those derived by NMR, CD, and predictive methods. The principal framework of the molecule is provided by two disulfide bonds, one ...
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    Predatory marine snails of the genus Conus paralyze their fish prey by injecting a potent toxin. The α-conotoxin GI is a 13-residue peptide isolated from venom of Conus geographus. It functions by blocking the postsynaptic nicotinic acetylcholine receptor. After crystallization in deionized water, the three-dimensional structure of the GI neurotoxin was determined to 1.2 Å resolution by X-ray crystallography. This structure, which can be described as a trianglar slab, shows overall similarities to those derived by NMR, CD, and predictive methods. The principal framework of the molecule is provided by two disulfide bonds, one linking Cys 2 and Cys 7 and the other Cys 3 and Cys 13. Opposite ends of the sequence are drawn together even further by hydrogen bonds between Glu 1 and Cys 13 and between Cys 2 and Ser 12. Since the C-terminus is amidated, only one negative charge is present (carboxylate of Glu 1), and this is not implicated in receptor binding. Two positively charged regions (the α-amino group of Glu 1 and the guanido group of Arg 9) are situated 15 Å apart at the corners of the triangular face of the molecule. φ,ψ angles characteristic of a 310 helix were observed for residues 5−7. For residues 8−11, these angles were consistent with either a type I β-turn or a distorted 310 helix.
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    Journal Title
    Biochemistry
    Volume
    35
    Issue
    35
    DOI
    https://doi.org/10.1021/bi960820h
    Subject
    Medicinal and biomolecular chemistry
    Biochemistry and cell biology
    Biochemistry and cell biology not elsewhere classified
    Medical biochemistry and metabolomics
    Publication URI
    http://hdl.handle.net/10072/347911
    Collection
    • Journal articles

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