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1ad7

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(New page: 200px<br /><applet load="1ad7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ad7" /> '''NMR STRUCTURE OF METAL-FREE CONANTOKIN G, 1 ...)
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'''NMR STRUCTURE OF METAL-FREE CONANTOKIN G, 1 STRUCTURE'''<br />
'''NMR STRUCTURE OF METAL-FREE CONANTOKIN G, 1 STRUCTURE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1AD7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_geographus Conus geographus] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AD7 OCA].
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1AD7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Conus_geographus Conus geographus] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AD7 OCA].
==Reference==
==Reference==
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[[Category: Conus geographus]]
[[Category: Conus geographus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Baleja, J.D.]]
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[[Category: Baleja, J D.]]
[[Category: Furie, B.]]
[[Category: Furie, B.]]
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[[Category: Furie, B.C.]]
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[[Category: Furie, B C.]]
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[[Category: Rigby, A.C.]]
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[[Category: Rigby, A C.]]
[[Category: NH2]]
[[Category: NH2]]
[[Category: conantokin g]]
[[Category: conantokin g]]
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[[Category: gamma-carboxyglutamic acid]]
[[Category: gamma-carboxyglutamic acid]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 10:46:07 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:43:15 2008''

Revision as of 09:43, 21 February 2008


1ad7

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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 with as ligand. 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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