恢复蛋白Recoverin正则模式分析的理论研究  

Theoretical Investigation of Recoverin′s Normal Mode Analysis

作　　者：李吉来[1,2] 耿彩云[2] 步宇翔[1] 陈效华[1] 王军[1] 黄旭日[2] 孙家锺[2] 

机构地区：[1]山东大学化学与化工学院,胶体与界面化学教育部重点实验室,济南250100 [2]吉林大学理论化学研究所,理论化学计算国家重点实验室,长春130021

出　　处：《高等学校化学学报》2009年第10期2055-2058,共4页Chemical Journal of Chinese Universities

基　　金：国家自然科学基金(批准号:20773048,200702019,20070421075);山东省博士后创新基金;中国博士后科学基金资助

摘　　要：采用旋转平移块方法对Ca2+/豆蔻酰基开关进行了正则模式分析(NMA).研究结果表明,恢复蛋白(Recoverin)的T态的N-末端与C-末端易于发生刚体逆向旋转,一旦结合Ca2+,很容易发生构象变化,形成具有双向构象转变特征的I态.I态是一个中间结构,既可以发生构象回转到T态,又可以继续相对旋转到R态,使豆蔻酰基完全暴露,从而行使其信号传导生物功能.从低频振动模式分析可以看出,恢复蛋白具有构象转变这一本质属性.Recoverin is an important branch of neuronal calcium sensor. It had been shown recently that half of the known protein movements can be modelled by using at most two low-frequency normal modes. Hence, we investigated their normal modes by rotational translational block method in order to give a deep insight into the nature of the Ca^2＋-myristoyl switch conformational transition. The normal mode perturbed models of recoverin T-state revealed that the overall motion of the first lowest mode could be described approximately as a converse-rigid-body-swivel around the inter-domain linker. While in the one Ca^2＋ -bound structure, in addition to the converse-rigid-body-swivel motion, an exposure of the myristoyl group is also detected, which was pro- posed as bidirectional conformational transition across the domain interface and facilitates the allosteric transition in signal-transduction processes. These observations indicate that reeoverin is intrinsically dynamic.

关 键 词：变构过程 信号传导 正则模式分析 低频振动 

分 类 号：O641[理学—物理化学]