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1ad7

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Revision as of 23:37, 21 October 2015

NMR STRUCTURE OF METAL-FREE CONANTOKIN G, 1 STRUCTURE

Structural highlights

1ad7 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[CKG_CONGE] Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors. This toxin is selective for the NR2B/GRIN2B subunit. Induces sleep-like symptoms in young mice and hyperactivity in older mice.^[1]

Publication Abstract from PubMed

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Olivera BM, Rivier J, Clark C, Ramilo CA, Corpuz GP, Abogadie FC, Mena EE, Woodward SR, Hillyard DR, Cruz LJ. Diversity of Conus neuropeptides. Science. 1990 Jul 20;249(4966):257-63. PMID:2165278
↑ Rigby AC, Baleja JD, Furie BC, Furie B. Three-dimensional structure of a gamma-carboxyglutamic acid-containing conotoxin, conantokin G, from the marine snail Conus geographus: the metal-free conformer. Biochemistry. 1997 Jun 10;36(23):6906-14. PMID:9188685 doi:10.1021/bi970321w

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ad7"

@@ Line 2: / Line 2: @@
 <StructureSection load='1ad7' size='340' side='right' caption='[[1ad7]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ad7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Conge Conge]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AD7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ad7]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AD7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AD7 FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
 <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ad7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ad7 OCA], [http://pdbe.org/1ad7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ad7 RCSB], [http://www.ebi.ac.uk/pdbsum/1ad7 PDBsum]</span></td></tr>
@@ Line 21: / Line 21: @@
 __TOC__
 </StructureSection>
-[[Category: Conge]]
 [[Category: Baleja, J D]]
 [[Category: Furie, B]]

1ad7

From Proteopedia

Revision as of 23:37, 21 October 2015

NMR STRUCTURE OF METAL-FREE CONANTOKIN G, 1 STRUCTURE

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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