1onu
From Proteopedia
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'''NMDA RECEPTOR ANTAGONIST, CONANTOKIN-G, NMR, 17 STRUCTURES''' | '''NMDA RECEPTOR ANTAGONIST, CONANTOKIN-G, NMR, 17 STRUCTURES''' | ||
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[[Category: Nielsen, K J.]] | [[Category: Nielsen, K J.]] | ||
[[Category: Skjaerbaek, N.]] | [[Category: Skjaerbaek, N.]] | ||
| - | [[Category: | + | [[Category: Antagonist]] |
| - | [[Category: | + | [[Category: Conantokin-t]] |
| - | [[Category: | + | [[Category: Nmda receptor]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:04:51 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:04, 3 May 2008
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 Page seeded by OCA on Sat May 3 04:04:51 2008
