2GZB

Bauhinia bauhinioides cruzipain inhibitor (BbCI)

2GZB の概要

• エントリーDOI: 10.2210/pdb2gzb/pdb
• 関連するPDBエントリー: 2GO2
• 分子名称: Kunitz-type proteinase inhibitor BbCI, IODIDE ION (3 entities in total)
• 機能のキーワード: cruzipain, kunitz, cysteine proteinase inhibitor, hydrolase inhibitor
• 由来する生物種: Bauhinia bauhinioides
• 細胞内の位置: Secreted: P83051
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37918.56

構造登録者

Hansen, D.,Macedo-Ribeiro, S.,Navarro, M.V.A.S.,Garratt, R.C.,Oliva, M.L.V. (登録日: 2006-05-11, 公開日: 2007-07-17, 最終更新日: 2024-04-03)

主引用文献

Hansen, D.,Macedo-Ribeiro, S.,Verissimo, P.,Yoo Im, S.,Sampaio, M.U.,Oliva, M.L.
Crystal structure of a novel cysteinless plant Kunitz-type protease inhibitor.
Biochem.Biophys.Res.Commun., 360:735-740, 2007

PubMed Abstract: Bauhinia bauhinioides Cruzipain Inhibitor (BbCI) is a cysteine protease inhibitor highly homologous to plant Kunitz-type inhibitors. However, in contrast to classical Kunitz family inhibitors it lacks cysteine residues and therefore disulfide bridges. BbCI is also distinct in the ability to inactivate enzymes belonging to two different classes, cysteine and serine proteases. Besides inhibiting the cysteine protease cruzipain, BbCI also inhibits cathepsin L and the serine proteases HNE (human neutrophil elastase) and PPE (porcine pancreatic elastase). Monoclinic crystals of the recombinant inhibitor that diffract to 1.7A resolution were obtained using hanging drop method by vapor diffusion at 18 degrees C. The refined structure shows the conservative beta-trefoil fold features of the Kunitz inhibitors. In BbCI, one of the two characteristic S-S bonds is replaced by the water-mediated interaction between Tyr125 and Gly132. In this work we explore the structural differences between Kunitz-type inhibitors and analyze the essential interactions that maintain the protein structural stability preserving its biological function.

PubMed: 17631863
DOI: 10.1016/j.bbrc.2007.06.144

実験手法

X-RAY DIFFRACTION (1.7 Å)