Hackney D D
Department of Biological Sciences, Carnegie Mellon University, Pittsburgh, PA 15214, USA.
Chem Biol. 1996 Jul;3(7):525-8. doi: 10.1016/s1074-5521(96)90142-8.
The recent solution of the crystal structure of the kinesin motor domain reveals striking similarities to the core region of the myosin motor domain, implying a strong evolutionary relationship between these two motors. However, a complete understanding of the way that motility is generated will require additional structural information, which may explain how the two motors have adapted to their fundamentally different linear substrates, F-actin and microtubules.
驱动蛋白运动结构域晶体结构的最新解析结果显示,它与肌球蛋白运动结构域的核心区域有着惊人的相似性,这意味着这两种分子马达之间存在着紧密的进化关系。然而,要全面理解产生运动的方式,还需要更多的结构信息,这些信息或许能解释这两种分子马达是如何适应它们截然不同的线性底物——肌动蛋白丝和微管的。