1IEN

SOLUTION STRUCTURE OF TIA

1IEN の概要

• エントリーDOI: 10.2210/pdb1ien/pdb
• 関連するPDBエントリー: 1IEO
• 分子名称: PROTEIN TIA (1 entity in total)
• 機能のキーワード: conotoxin, alpha1-adrenoceptors, toxin
• 細胞内の位置: Secreted: P58811
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2399.95

構造登録者

Sharpe, I.A.,Gehrmann, J.,Loughnan, M.L.,Thomas, L.,Adams, D.A.,Atkins, A.,Palant, E.,Craik, D.J.,Adams, D.J.,Alewood, P.F.,Lewis, R.J. (登録日: 2001-04-10, 公開日: 2002-04-03, 最終更新日: 2022-02-23)

主引用文献

Sharpe, I.A.,Gehrmann, J.,Loughnan, M.L.,Thomas, L.,Adams, D.A.,Atkins, A.,Palant, E.,Craik, D.J.,Adams, D.J.,Alewood, P.F.,Lewis, R.J.
Two new classes of conopeptides inhibit the alpha1-adrenoceptor and noradrenaline transporter.
Nat.Neurosci., 4:902-907, 2001

PubMed Abstract: Cone snails use venom containing a cocktail of peptides ('conopeptides') to capture their prey. Many of these peptides also target mammalian receptors, often with exquisite selectivity. Here we report the discovery of two new classes of conopeptides. One class targets alpha1-adrenoceptors (rho-TIA from the fish-hunting Conus tulipa), and the second class targets the neuronal noradrenaline transporter (chi-MrIA and chi-MrIB from the mollusk-hunting C. marmoreus). rho-TIA and chi-MrIA selectively modulate these important membrane-bound proteins. Both peptides act as reversible non-competitive inhibitors and provide alternative avenues for the identification of inhibitor drugs.

PubMed: 11528421
DOI: 10.1038/nn0901-902

実験手法

SOLUTION NMR