捕食线虫真菌丝氨酸蛋白酶PII结构的同源模建  

Structure Homology Modeling of Nematode-Trapping Fungus Serine Protease PII

作　　者：杨力权[1,2] 桑鹏[2] 李珍贵[1] 

机构地区：[1]大理学院农学与生物科学学院,云南大理671003 [2]云南大学云南省生物资源保护与利用重点实验室,昆明650091

出　　处：《大理学院学报（综合版）》2013年第10期41-43,共3页Journal of Dali University

基　　金：云南省教育厅基金资助项目(2012Y150)

摘　　要：通过同源模建方法构建捕食线虫真菌丝氨酸蛋白酶PII的三维结构模型,并结合以往研究对其结构进行分析。结果表明,蛋白酶PII的结构具有枯草杆菌丝氨酸蛋白酶特有的α/β脚手架折叠模式,具有保守的催化三聚体和氧负离子孔结构组织,整体表现为坚固的球状折叠构型,不具备二硫键。研究结果将为进一步深入研究PII的结构和功能之间的关系奠定结构基础。In this article, structural model of Nematode-trapping fungus serine protease PII is constructed and analyzed. The results show that the structural model of PII has the common ct/[3 scaffold characteristics of subtilisin-like serine protease. The catalytic triad residues Asp, His and Ser and the component of oxianion hole residue Asn are completely conserved. The structural model has an over- all highly rigid globular fold architecture and do not have disulfide bond. The results of this article will provide a solid basis for further studying the relationship between structure and function of PII.

关 键 词：丝氨酸蛋白酶PII 结构模型 同源模建 结构功能研究 

分 类 号：O623[理学—有机化学] R378.996[理学—化学]