目的同源模建E1蛋白及其受体髓鞘少突胶质细胞糖蛋白(myelin oligodendrocyte glycoprotein,MOG)的三维结构,应用分子对接的方法预测E1蛋白与其受体MOG的候选结合氨基酸残基。方法采用MODELLER程序预测E1蛋白及其受体MOG的三维结构,并应用CASTp server进行活性口袋的预测;采用ProtScale进行疏水性分析,应用基于隐马尔可夫模型(HMM)算法的SMART程序搜索蛋白序列的motif;采用PyMOL-APBS软件设计E1蛋白及其受体MOG分子的腔介质结构,分析其表观静电势,应用PLATINUM程序进行分子对接,寻找其结合位点。结果 E1蛋白由3个结构域组成,其中D1、D3处于结构的底部,形成一个大的口袋,C-末端与D2的一侧形成另一个大的口袋,其余口袋主要集中在D2上半部的融合面中;MOG的结构模型为8个反平行的β折叠组成的一个β折叠桶,预测结构的主链构象的所有氨基酸均处于允许区。在MOG N-末端1~17位的氨基酸残基形成一个motif(low complexity region),46~127位的氨基酸残基形成了一个motif V型免疫球蛋白样结构域(Immunoglobulin V-Type,IGv);low complexity region段氨基酸残基表现为强疏水性。MOG N-末端的5个残基基序及ARG101~GLU107构成的β转角共同形成一个突起的结构,插入到E1蛋白的活性口袋中,与口袋中的ALA86、TYR90、TYR101、PHE102、ASN103、GLY105、SER107、TYR109、ALA122、PHE123、HIS125、SER126相互结合。结论应用计算机模拟技术预测了E1蛋白与其受体MOG结合的特定结合域,为今后进一步研究其相互作用奠定了基础。 OBJECTIVE: To construct the three-dimensional structure of E1 protein and its receptor myelin oligodendrocyte glycoprotein (MOG) by homology modeling and to predict the candidate binding amino acid residues of E1 protein and its receptor MOG by molecular docking. Methods The three-dimensional structure of E1 protein and its receptor MOG was predicted by MODELLER program and CASTp server was used to predict the active pocket. Hydrophobic analysis was performed using ProtScale. SMART program based on Hidden Markov Model (HMM) algorithm was used to search for protein sequence The motif of the E1 protein and its receptor MOG was designed by PyMOL-APBS software. The apparent electrostatic potential was analyzed. The PLATINUM program was used for molecular docking to find the binding sites. Results The E1 protein consisted of three domains, with D1 and D3 at the bottom of the structure, forming a large pocket with another large pocket at the C-terminus and one side of D2, with the remaining pocket mainly concentrated in the upper half of D2 In the fusion surface, the structural model of MOG is a β-folding barrel composed of eight antiparallel β-sheets, and all the amino acids in the main-chain conformation of the structure are predicted to be in the allowable region. A motif (low complexity region) is formed in the amino acid residues 1 to 17 at the N-terminal of MOG, and a motif V immunoglobulin V-type (IGv) is formed in amino acid residues 46 to 127 ; low complexity region Amino acid residues show strong hydrophobicity. The 5 residues motif at the N-terminus of MOG and the β-turn formed by ARG101 ~ GLU107 together form a protuberant structure, which is inserted into the active pocket of E1 protein and interacts with ALA86, TYR90, TYR101, PHE102, ASN103, GLY105 , SER107, TYR109, ALA122, PHE123, HIS125, SER126. Conclusions The specific binding domains of E1 protein and its receptor MOG are predicted by computer simulation technology, which lays the foundation for further study of its interaction in the future.