1not: Difference between revisions

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[[Image:1not.gif|left|200px]]
{{Seed}}
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{{STRUCTURE_1not|  PDB=1not  |  SCENE=  }}  
{{STRUCTURE_1not|  PDB=1not  |  SCENE=  }}  


'''THE 1.2 ANGSTROM STRUCTURE OF G1 ALPHA CONOTOXIN'''
===THE 1.2 ANGSTROM STRUCTURE OF G1 ALPHA CONOTOXIN===




==Overview==
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Predatory marine snails of the genus Conus paralyze their fish prey by injecting a potent toxin. The alpha-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 A resolution by X-ray crystallography. This structure, which can be described as a triangular 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 alpha-amino group of Glu 1 and the guanido group of Arg 9) are situated 15 A apart at the corners of the triangular face of the molecule. phi, psi angles characteristic of a 3(10) helix were observed for residues 5-7. For residues 8-11, these angles were consistent with either a type I beta-turn or a distorted 3(10) helix.
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{{ABSTRACT_PUBMED_8784187}}


==About this Structure==
==About this Structure==
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[[Category: Disulphide loop]]
[[Category: Disulphide loop]]
[[Category: Venom]]
[[Category: Venom]]
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