2H7Z

Crystal structure of irditoxin

2H7Z の概要

• エントリーDOI: 10.2210/pdb2h7z/pdb
• 分子名称: Irditoxin subunit A, Irditoxin subunit B (3 entities in total)
• 機能のキーワード: three-finger toxin, neurotoxin, snake venom, toxin
• 由来する生物種: Boiga irregularis; 詳細
• 細胞内の位置: Secreted: A0S864 A0S865
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17112.41

構造登録者

Pawlak, J.,Kini, R.M.,Stura, E.A.,Le Du, M.H. (登録日: 2006-06-06, 公開日: 2006-08-29, 最終更新日: 2024-11-13)

主引用文献

Pawlak, J.,Mackessy, S.P.,Sixberry, N.M.,Stura, E.A.,Le Du, M.H.,Menez, R.,Foo, C.S.,Menez, A.,Nirthanan, S.,Kini, R.M.
Irditoxin, a novel covalently linked heterodimeric three-finger toxin with high taxon-specific neurotoxicity.
Faseb J., 23:534-545, 2009

PubMed Abstract: A novel heterodimeric three-finger neurotoxin, irditoxin, was isolated from venom of the brown treesnake Boiga irregularis (Colubridae). Irditoxin subunit amino acid sequences were determined by Edman degradation and cDNA sequencing. The crystal structure revealed two subunits with a three-finger protein fold, typical for "nonconventional" toxins such as denmotoxin, bucandin, and candoxin. This is the first colubrid three-finger toxin dimer, covalently connected via an interchain disulfide bond. Irditoxin showed taxon-specific lethality toward birds and lizards and was nontoxic toward mice. It produced a potent neuromuscular blockade at the avian neuromuscular junction (IC(50)=10 nM), comparable to alpha-bungarotoxin, but was three orders of magnitude less effective at the mammalian neuromuscular junction. Covalently linked heterodimeric three-finger toxins found in colubrid venoms constitute a new class of venom peptides, which may be a useful source of new neurobiology probes and therapeutic leads.

PubMed: 18952712
DOI: 10.1096/fj.08-113555

実験手法

X-RAY DIFFRACTION (1.5 Å)