1IMT

MAMBA INTESTINAL TOXIN 1, NMR, 39 STRUCTURES

1IMT の概要

• エントリーDOI: 10.2210/pdb1imt/pdb
• 分子名称: INTESTINAL TOXIN 1 (1 entity in total)
• 機能のキーワード: venom, structural homologue of colipase, resistance to endoproteases, contract guinea pig ileum, toxin
• 由来する生物種: Dendroaspis polylepis polylepis (black mamba)
• 細胞内の位置: Secreted: P25687
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8531.04

構造登録者

Boisbouvier, J.,Albrand, J.-P.,Blackledge, M.,Jaquinod, M.,Schweitz, H.,Lazdunski, M.,Marion, D. (登録日: 1998-04-14, 公開日: 1999-04-20, 最終更新日: 2024-11-20)

主引用文献

Boisbouvier, J.,Albrand, J.P.,Blackledge, M.,Jaquinod, M.,Schweitz, H.,Lazdunski, M.,Marion, D.
A structural homologue of colipase in black mamba venom revealed by NMR floating disulphide bridge analysis.
J.Mol.Biol., 283:205-219, 1998

PubMed Abstract: The solution structure of mamba intestinal toxin 1 (MIT1), isolated from Dendroaspis polylepis polylepis venom, has been determined. This molecule is a cysteine-rich polypeptide exhibiting no recognised family membership. Resistance to MIT1 to classical specific endoproteases produced contradictory NMR and biochemical information concerning disulphide-bridge topology. We have used distance restraints allowing ambiguous partners between S atoms in combination with NMR-derived structural information, to correctly determine the disulphide-bridge topology. The resultant solution structure of MIT1, determined to a resolution of 0.5 A, reveals an unexpectedly similar global fold with respect to colipase, a protein involved in fatty acid digestion. Colipase exhibits an analogous resistance to endoprotease activity, indicating for the first time the possible topological origins of this biochemical property. The biochemical and structural homology permitted us to propose a mechanically related digestive function for MIT1 and provides novel information concerning snake venom protein evolution.

PubMed: 9761684
DOI: 10.1006/jmbi.1998.2057

実験手法

SOLUTION NMR