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作 者:薛晓怡[1] 冯铁男[1] 王群群[1] 王翼飞[1]
机构地区:[1]上海大学理学院,上海200444
出 处:《上海大学学报(自然科学版)》2011年第6期728-733,共6页Journal of Shanghai University:Natural Science Edition
基 金:国家自然科学基金资助项目(30871341);上海市重点学科建设资助项目(S30104);上海市教委重点学科建设资助项目(J50101)
摘 要:P311蛋白广泛表达于多种组织,并参与体内细胞分化、调节其他蛋白/基因转录、创伤修复、肿瘤发生等多种正常或异常的生物学活动.研究发现,金属硫蛋白ⅡA(metallothionein ⅡA,MT2A)参与P311基因的表达,并起着关键性的调节作用,这说明二者存在着相互作用的关系.采用同源建模的方法构建P311蛋白的3D结构,使用Autodock 4.0软件将结构模型与MT2A进行分子对接,模拟蛋白质间的相互作用,预测二者的作用区域,找出可能的关键残基GLU14,SER48以及GLU56,为进一步的实验研究奠定基础.P311 was identified by suppressive subtraction hybridization as potentially involved in smooth muscle myogenesis. The P311 expression is regulated at multiple levels by pathways that control cellular transformation. It has been demonstrated in the literature that metallothionein ⅡA (MT2A) is associated with the expression of P311, and it is critical in the regulation. Therefore, it has been considered that interaction between P311 and MT2A exists. A 3D model of P311 protein by homology modeling is constructed, and the related residues for interaction are analyzed with Autodock 4.0. The results show that amino acids such as GLU14, SER48 and GLU56 are important in binding, which forms a basis for further experiments.
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