Is the dynein motor a winch?
Is the dynein motor a winch?
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DOI：
10.1016/j.sbi.2004.03.013
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发表时间：
2004-04-01
影响因子：
6.8
通讯作者：
Knight, PJ
中科院分区：
文献类型：
--
作者：
Burgess, SA;Knight, PJ
动力蛋白是真核细胞中三类线性运动蛋白中最大、最复杂的。动力蛋白运动域的质量大约是其他微管运动蛋白驱动蛋白的十倍。动力蛋白与机械酶 AAA+ 超家族的同源性使其有别于驱动蛋白和肌球蛋白，后者作为 G 蛋白超家族的成员具有共同的折叠和祖先。与其他运动蛋白相比，人们对动力蛋白的机制知之甚少。即使在低分辨率下，其三维结构也是未知的。最近的电子显微镜二维图像揭示了其结构的新细节以及它如何变化以产生运动。这些以及最近解决的另一种 AAA+ 蛋白 ClpB 的晶体结构，为动力蛋白的机制提供了诱人的线索，表明它可能像分子一样发挥作用。
Dyneins are the largest and most complex of the three classes of linear motor proteins in eukaryotic cells. The mass of the dynein motor domain is about ten times that of the other microtubule motor, kinesin. Dynein's homology with the AAA+ superfamily of mechanoenzymes distinguishes it from both kinesin and myosin, which share a common fold and ancestry as members of the G-protein superfamily. In contrast to the other motor proteins, little is known about the mechanism of dynein; its three-dimensional structure is unknown even at low resolution. Recent two-dimensional images from electron microscopy have revealed new details of its structure and how this changes to produce movement. These and the recently solved crystal structure of another AAA+ protein, ClpB, offer tantalising hints about dynein's mechanism, suggesting it may act like a molecular