1not: Difference between revisions
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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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| 1not, resolution 1.2Å | |||||||||||||
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| Ligands: | NH2 | ||||||||||||
| 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
Page seeded by OCA on Thu Mar 20 12:59:39 2008
