CAJ | 학술논문

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。
통과동원모건방법구건포식선충진균사안산단백매PII적삼유결구모형，병결합이왕연구대기결구진행분석。결과표명，단백매PII적결구구유고초간균사안산단백매특유적α/β각수가절첩모식，구유보수적최화삼취체화양부리자공결구조직，정체표현위견고적구상절첩구형，불구비이류건。연구결과장위진일보심입연구PII적결구화공능지간적관계전정결구기출。
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 commonα/βscaffold 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.