【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.更多还原

【Abstract】 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 Ca2+-myristoyl switch conformational transition.The normal mode perturbed models of reco-verin 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 Ca2+-bound structure,in addition to the converse-rigid-body-swivel motion,an exposure of the myristoyl group is also detected,which was proposed as bidirectional conformational transition across the domain interface and facilitates the allosteric transition in signal-transduction processes.These observations indicate that recoverin is intrinsically dynamic.更多还原