1onu
From Proteopedia
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|PDB= 1onu |SIZE=350|CAPTION= <scene name='initialview01'>1onu</scene> | |PDB= 1onu |SIZE=350|CAPTION= <scene name='initialview01'>1onu</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=CGU:GAMMA-CARBOXY-GLUTAMIC+ACID'>CGU</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1onu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1onu OCA], [http://www.ebi.ac.uk/pdbsum/1onu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1onu RCSB]</span> | ||
}} | }} | ||
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[[Category: Nielsen, K J.]] | [[Category: Nielsen, K J.]] | ||
[[Category: Skjaerbaek, N.]] | [[Category: Skjaerbaek, N.]] | ||
| - | [[Category: NH2]] | ||
[[Category: antagonist]] | [[Category: antagonist]] | ||
[[Category: conantokin-t]] | [[Category: conantokin-t]] | ||
[[Category: nmda receptor]] | [[Category: nmda receptor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:47:56 2008'' |
Revision as of 19:47, 30 March 2008
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMDA RECEPTOR ANTAGONIST, CONANTOKIN-G, NMR, 17 STRUCTURES
Overview
Conantokin-G and conantokin-T are two paralytic polypeptide toxins originally isolated from the venom of the fish-hunting cone snails of the genus Conus. Conantokin-G and conantokin-T are the only naturally occurring peptidic compounds which possess N-methyl-D-aspartate receptor antagonist activity, produced by a selective non-competitive antagonism of polyamine responses. They are also structurally unusual in that they contain a disproportionately large number of acid labile post-translational gamma-carboxyglutamic acid (Gla) residues. Although no precise structural information has previously been published for these peptides, early spectroscopic measurements have indicated that both conantokin-G and conantokin-T form alpha-helical structures, although there is some debate whether the presence of calcium ions is required for these peptides to adopt this fold. We now report a detailed structural study of synthetic conantokin-G and conantokin-T in a range of solution conditions using CD and 1H NMR spectroscopy. The three-dimensional structures of conantokin-T and conantokin-G were calculated from 1H NMR-derived distance and dihedral restraints. Both conantokins were found to contain a mixture of alpha- and 310 helix, that give rise to curved and straight helical conformers. Conantokin-G requires the presence of divalent cations (Zn2+, Ca2+, Cu2+, or Mg2+) to form a stable alpha-helix, while conantokin-T adopts a stable alpha-helical structure in aqueous conditions, in the presence or absence of divalent cations (Zn2+, Ca2+, Cu2+, or Mg2+).
About this Structure
1ONU is a Single protein structure of sequence from Conus geographus. Full crystallographic information is available from OCA.
Reference
Determination of the solution structures of conantokin-G and conantokin-T by CD and NMR spectroscopy., Skjaerbaek N, Nielsen KJ, Lewis RJ, Alewood P, Craik DJ, J Biol Chem. 1997 Jan 24;272(4):2291-9. PMID:8999936
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