1ad7
From Proteopedia
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- | [[Image:1ad7.gif|left|200px]] | + | [[Image:1ad7.gif|left|200px]] |
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- | '''NMR STRUCTURE OF METAL-FREE CONANTOKIN G, 1 STRUCTURE''' | + | {{Structure |
+ | |PDB= 1ad7 |SIZE=350|CAPTION= <scene name='initialview01'>1ad7</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''NMR STRUCTURE OF METAL-FREE CONANTOKIN G, 1 STRUCTURE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1AD7 is a [ | + | 1AD7 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=1AD7 OCA]. |
==Reference== | ==Reference== | ||
- | Three-dimensional structure of a gamma-carboxyglutamic acid-containing conotoxin, conantokin G, from the marine snail Conus geographus: the metal-free conformer., Rigby AC, Baleja JD, Furie BC, Furie B, Biochemistry. 1997 Jun 10;36(23):6906-14. PMID:[http:// | + | Three-dimensional structure of a gamma-carboxyglutamic acid-containing conotoxin, conantokin G, from the marine snail Conus geographus: the metal-free conformer., Rigby AC, Baleja JD, Furie BC, Furie B, Biochemistry. 1997 Jun 10;36(23):6906-14. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9188685 9188685] |
[[Category: Conus geographus]] | [[Category: Conus geographus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gamma-carboxyglutamic acid]] | [[Category: gamma-carboxyglutamic acid]] | ||
- | ''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 09:55:55 2008'' |
Revision as of 07:55, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
NMR STRUCTURE OF METAL-FREE CONANTOKIN G, 1 STRUCTURE
Overview
Conantokin G is a gamma-carboxyglutamic acid-containing conotoxin from the venom of the marine cone snail Conus geographus. The 17-residue peptide, which contains five gamma-carboxyglutamic acid (Gla) residues and an amidated C-terminal asparagine amide, was synthesized chemically in a form identical to the natural conantokin G. To gain insight into the role of gamma-carboxyglutamic acid in the structure of this peptide, we determined the three-dimensional structure of conantokin G by 1H NMR and compared its structure to other conotoxins and to the gamma-carboxyglutamic acid-containing regions of the vitamin K-dependent blood-clotting proteins. Complete resonance assignments were made by two-dimensional 1H NMR spectroscopy in the absence of metal ions. NOE cross-peaks d(alphaN), d(NN), and d(betaN) provided interproton distance information, and vicinal spin-spin coupling constants 3J(HN alpha) were used to calculate phi torsion angles. Distance geometry and simulated annealing methods were used to derive 20 convergent structures from a set of 227 interproton distance restraints and 13 torsion angle measurements. The backbone rmsd to the geometric average for 20 final structures is 0.8 +/- 0.1 A. Conantokin G consists of a structured region commencing at Gla 3 and extending through arginine 13. This structure includes a partial loop centered around Gla 3 and Gla 4, a distorted type I turn between glutamine 6 and glutamine 9, and two type I turns involving Gla 10, leucine 11, and isoleucine 12 and arginine 13. Together, these two turns define approximately 1.6 turns of a distorted 3(10) helix. The observed structure possesses structural elements similar to those seen in the disulfide-linked conotoxins.
About this Structure
1AD7 is a Single protein structure of sequence from Conus geographus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of a gamma-carboxyglutamic acid-containing conotoxin, conantokin G, from the marine snail Conus geographus: the metal-free conformer., Rigby AC, Baleja JD, Furie BC, Furie B, Biochemistry. 1997 Jun 10;36(23):6906-14. PMID:9188685
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