用分子模拟方法研究大戟科抗HIV病毒蛋白与腺嘌呤的识别及其运动性  

Study on the Recognition and Motion of GAP31 with Adenine Via Molecule Simulation Methods

作　　者：胡建平[1] 刘嵬[2] 张智锦[1] 范晶[1] 唐典勇[1] 

机构地区：[1]乐山师范学院化学与生命科学学院,四川乐山614004 [2]成都大学药食同源植物资源开发重点实验室,成都610106

出　　处：《生物物理学报》2011年第10期875-882,共8页Acta Biophysica Sinica

基　　金：四川省中医药管理局科技专项(201003);四川省教育厅基金项目(08ZB054)~~

摘　　要：大戟科抗HIV病毒蛋白(GAP31)能有效地抑制HIV-1整合酶的整合功能,是一种潜在的抗AIDS药物。作者对GAP31蛋白与其底物腺嘌呤(adenine,ADE)的复合物进行了5 ns的分子动力学模拟,从能量和氢键两个角度详细分析了GAP31与ADE识别中的关键残基。结果表明,ADE主要结合在GAP31的T71～V80、G111～K120、I161～F170及F87所构成的口袋中,模拟结果与实验吻合。最后,分子整体运动性结果说明,分子的构象变化更多地与糖基化相关,与其抑制整合酶的活性关系不大。Gelonium anti-HIV protein（GAP31） effectively inhibits the integration function of HIV-1 integrase,thus is a potential anti-AIDS drug.One molecular dynamics simulation of 5 ns was performed for GAP31 complexed with its substrate adenine（ADE）.The key residues in the recognition of GAP31 with ADE were detailedly analyzed from the energy and hydrogen-bond aspects.The results show that ADE binds to the pocket composed by the residues from T71 to V80,G111 to K120,I161 to F170 and F87 of GAP31.All the modeling results agree well with experimental data.Finally,the whole molecule motion shows that the conformation change has some correlation with its glycosylation function,while irrelevant with the enzymatic inhibition of integrase.

关 键 词：GAP31 腺嘌呤 分子动力学模拟 构象 

分 类 号：Q615[生物学—生物物理学]