捕食线虫真菌丝氨酸蛋白酶PII结构的同源模建

J4 ›› 2013, Vol. 12 ›› Issue (10): 41-43.

捕食线虫真菌丝氨酸蛋白酶PII结构的同源模建

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

收稿日期:2013-06-01 修回日期:2013-07-03 出版日期:2013-10-15 发布日期:2013-10-15
作者简介:杨力权，讲师，博士研究生，主要从事结构生物学研究.
基金资助:
云南省教育厅基金资助项目（2012Y150）

Structure Homology Modeling of Nematode-Trapping Fungus Serine Protease PII

1. College of Agriculture and Biology Science, Dali University, Dali,Yunnan 671003, China;2.Laboratory for Conservation and Utilization of Bio-Resources & Key Laboratory for Microbial Resources of the Ministry of Education, Yunnan University, Kunming 650091, China

Received:2013-06-01 Revised:2013-07-03 Online:2013-10-15 Published:2013-10-15

摘要/Abstract

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。

关键词: 丝氨酸蛋白酶PII, 结构模型, 同源模建, 结构功能研究

Abstract:

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 α/β 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 overall 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.

Key words: serine protease PII, structural model, homology modeling, structure and function relationship

中图分类号:

杨力权, 桑鹏, 李珍贵. 捕食线虫真菌丝氨酸蛋白酶PII结构的同源模建[J]. J4, 2013, 12(10): 41-43.

YANG Li-Quan, SANG Peng, LI Zhen-Gui. Structure Homology Modeling of Nematode-Trapping Fungus Serine Protease PII[J]. J4, 2013, 12(10): 41-43.

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