2BI6

NMR STUDY OF BROMELAIN INHIBITOR VI FROM PINEAPPLE STEM

2BI6 の概要

• エントリーDOI: 10.2210/pdb2bi6/pdb
• 分子名称: BROMELAIN INHIBITOR VI (2 entities in total)
• 機能のキーワード: cysteine protease inhibitor
• 由来する生物種: Ananas comosus (pineapple); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 5885.80

構造登録者

Hatano, K.-I. (登録日: 1995-12-07, 公開日: 1996-04-03, 最終更新日: 2024-10-23)

主引用文献

Hatano, K.,Kojima, M.,Tanokura, M.,Takahashi, K.
Solution structure of bromelain inhibitor IV from pineapple stem: structural similarity with Bowman-Birk trypsin/chymotrypsin inhibitor from soybean.
Biochemistry, 35:5379-5384, 1996

PubMed Abstract: Bromelain inhibitor VI from pineapple stem (BI-VI) is a unique double-chain inhibitor with an 11-residue light chain and a 41-residue heavy chain by disulfide bonds and inhibits the cysteine proteinase bromelain competitively. The structure of BI-VI in aqueous solution was determined using nuclear magnetic resonance spectroscopy and simulated annealing-based calculations. Its three-dimensional structure was shown to be composed of two distinct domains, each of which is formed by a three-stranded antiparallel beta-sheet. Unexpectedly, BI-VI was found to share a similar folding and disulfide bond connectivities not with cystatin superfamily inhibitors which inhibit the same cysteine proteinases but with the Bowman-Birk trypsin/chymotrypsin inhibitor from soybean (BBI-I). BBI-I is a 71-residue inhibitor which has two independent inhibitory sites toward the serine proteinases trypsin and chymotrypsin. These structural similarities with BBI-I suggest that they have evolved from a common ancestor and differentiated in function during a course of molecular evolution.

PubMed: 8611527
DOI: 10.1021/bi952754+

実験手法

SOLUTION NMR