人SEPT9蛋白同源建模和活性位点分析

利用生物信息学在线软件预测了人SETP 9蛋白质的二级结构和模体信息,同时对其三级结构进行同源建模和模建结果质量评价,其次预测了该蛋白质的活性位点信息,旨在从蛋白质序列特征和分子结构水平理解其在人类生理病理过程中的作用.结果表明,模建的SEPT 9蛋白结构品质较高,具有7段α-螺旋和2组β-折叠结构,是一个典型的α/β类蛋白,表面呈弱正电势分布;人SEPT 9蛋白具有8个不同模体,可能参与不同生化反应或执行不同的功能.搜寻获得了人SEPT 9蛋白配基结合位点有10个,其中位点1可能是该蛋白的活性位点.这些研究结果对理解人SEPT 9蛋白功能以及配基结合位点定位非常重要,也为针对SEPT 9蛋白的分子对接和药物从头设计提供了理论基础.

Homology Modeling of Human SEPT9 Protein and Analysis of Its Active Site

To reveal the function of human SEPT 9protein in physiological and pathological process through protein sequence characteristics and molecule structure,its secondary structure,tertiary structures and motif were predicted by online website.And the structural quality of atomic model(3D)were assessed by Ramachandran graph and compatibility test of 3Dvs1Dstructure,then its active sites were predicted.The results showed that the tertiary structures of human SEPT 9protein with higher quality was obtained,it comprised sevenα-helix and two types ofβ-extended strand,belonged toα/βprotein,the surface in tertiary structure appeared weak positive charge.Eight different motif patters were found in amino acid sequence,which means that it may be involved in different biochemical reaction or perform different functions.At last,10different ligand-bing sites in its tertiary structures were found,and the first one may be its real active site.The results were very important to understand the function and to identify the location of ligand-binding sites for human SEPT 9protein,and also provided a basic information for molecular docking and de novo drug design.