1ONU
NMDA RECEPTOR ANTAGONIST, CONANTOKIN-G, NMR, 17 STRUCTURES
1ONU の概要
| エントリーDOI | 10.2210/pdb1onu/pdb |
| 分子名称 | CONANTOKIN-G (1 entity in total) |
| 機能のキーワード | nmda receptor, antagonist, conantokin-t |
| 由来する生物種 | Conus geographus (geography cone) |
| 細胞内の位置 | Secreted: P07231 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 2265.20 |
| 構造登録者 | Skjaerbaek, N.,Nielsen, K.J.,Lewis, R.J.,Alewood, P.F.,Craik, D.J. (登録日: 1996-08-27, 公開日: 1997-09-04, 最終更新日: 2022-02-23) |
| 主引用文献 | Skjaerbaek, N.,Nielsen, K.J.,Lewis, R.J.,Alewood, P.,Craik, D.J. Determination of the solution structures of conantokin-G and conantokin-T by CD and NMR spectroscopy. J.Biol.Chem., 272:2291-2299, 1997 Cited by PubMed Abstract: 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+). PubMed: 8999936DOI: 10.1074/jbc.272.4.2291 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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