期刊
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
卷 68, 期 -, 页码 794-799出版社
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S090744491201222X
关键词
-
资金
- Nederlandse Organisatie voor Wetenschappelijk Onderzoek (NWO) [021.002.024, 700.55.425]
Potato serine protease inhibitor (PSPI) constitutes about 22% of the total amount of proteins in potato tubers (cv. Elkana), making it the most abundant protease inhibitor in the plant. PSPI is a heterodimeric double-headed Kunitz-type serine protease inhibitor that can tightly and simultaneously bind two serine proteases by mimicking the substrate of the enzyme with its reactive-site loops. Here, the crystal structure of PSPI is reported, representing the first heterodimeric double-headed Kunitz-type serine protease inhibitor structure to be determined. PSPI has a beta-trefoil fold and, based on the structure, two reactive-site loops bearing residues Phe75 and Lys95 were identified.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据