1not
From Proteopedia
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- | [[Image:1not.gif|left|200px]] | + | [[Image:1not.gif|left|200px]] |
- | + | ||
- | '''THE 1.2 ANGSTROM STRUCTURE OF G1 ALPHA CONOTOXIN''' | + | {{Structure |
+ | |PDB= 1not |SIZE=350|CAPTION= <scene name='initialview01'>1not</scene>, resolution 1.2Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''THE 1.2 ANGSTROM STRUCTURE OF G1 ALPHA CONOTOXIN''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1NOT is a [ | + | 1NOT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Conus_geographus Conus geographus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NOT OCA]. |
==Reference== | ==Reference== | ||
- | Three-dimensional structure of the alpha-conotoxin GI at 1.2 A resolution., Guddat LW, Martin JA, Shan L, Edmundson AB, Gray WR, Biochemistry. 1996 Sep 3;35(35):11329-35. PMID:[http:// | + | Three-dimensional structure of the alpha-conotoxin GI at 1.2 A resolution., Guddat LW, Martin JA, Shan L, Edmundson AB, Gray WR, Biochemistry. 1996 Sep 3;35(35):11329-35. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8784187 8784187] |
[[Category: Conus geographus]] | [[Category: Conus geographus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: venom]] | [[Category: venom]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:59:39 2008'' |
Revision as of 10:59, 20 March 2008
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, resolution 1.2Å | |||||||
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Coordinates: | save as pdb, mmCIF, xml |
THE 1.2 ANGSTROM STRUCTURE OF G1 ALPHA CONOTOXIN
Overview
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.
About this Structure
1NOT is a Single protein structure of sequence from Conus geographus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the alpha-conotoxin GI at 1.2 A resolution., Guddat LW, Martin JA, Shan L, Edmundson AB, Gray WR, Biochemistry. 1996 Sep 3;35(35):11329-35. PMID:8784187
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