Expression, purification, crystallization and preliminary X-ray crystallographic analysis of human myosin 1c in complex with calmodulin.
Expression, purification, crystallization and preliminary X-ray crystallographic analysis of human myosin 1c in complex with calmodulin.
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人肌球蛋白1c与钙调蛋白复合物的表达、纯化、结晶和初步X射线晶体分析
DOI：
10.1107/s1744309113020988
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发表时间：
2013
期刊：
影响因子：
--
通讯作者：
D. J. Manstein
中科院分区：
文献类型：
--
作者：
S. Münnich;D. J. Manstein
肌球蛋白1c（Myo1c）涉及几个细胞过程，如囊泡运输和内耳适应的介导。因此，损害Myo1c运动活性的突变导致人类听力损失。为了在分子水平上理解Myo1c在该过程中的作用，测定了其与轻链钙调蛋白复合物的晶体结构。一个人Myo1c构建体，包括电机域和第一个IQ基序与钙调蛋白在Sf9细胞中共表达，并纯化至同质。蛋白质复合物容易结晶，晶体属于空间群P21，衍射分辨率为3 μ m。 目前正在尝试通过分子置换来确定其结构。
Myosin 1c (Myo1c) is implicated in several cellular processes such as vesicle transport and the mediation of adaptation in the inner ear. Consequently, mutations impairing Myo1c motor activity lead to hearing loss in humans. To understand the role of Myo1c in this process on a molecular level, its crystal structure in complex with the light chain calmodulin was determined. A human Myo1c construct encompassing the motor domain and the first IQ motif was co-expressed with calmodulin in Sf9 cells and purified to homogeneity. The protein complex crystallized readily, and the crystals belonged to space group P21 and diffracted to 3 Å resolution. Attempts to determine the structure by molecular replacement are currently under way.
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