Squire John M
Muscle Contraction Group, Department of Physiology and Pharmacology, University of Bristol, Bristol, BS8 1TD, UK.
Biophys Rev. 2009 Sep;1(3):149. doi: 10.1007/s12551-009-0017-4. Epub 2009 Sep 11.
Myosin filaments in muscle, carrying the ATPase myosin heads that interact with actin filaments to produce force and movement, come in multiple varieties depending on species and functional need, but most are based on a common structural theme. The now successful journeys to solve the ultrastructures of many of these myosin filaments, at least at modest resolution, have not been without their false starts and erroneous sidetracks, but the picture now emerging is of both diversity in the rotational symmetries of different filaments and a degree of commonality in the way the myosin heads are organised in resting muscle. Some of the remaining differences may be associated with how the muscle is regulated. Several proteins in cardiac muscle myosin filaments can carry mutations associated with heart disease, so the elucidation of myosin filament structure to understand the effects of these mutations has a clear and topical clinical relevance.
肌肉中的肌球蛋白丝带有与肌动蛋白丝相互作用以产生力量和运动的ATP酶肌球蛋白头部,根据物种和功能需求有多种类型,但大多数基于共同的结构主题。现在,至少以适度分辨率成功解析许多此类肌球蛋白丝超微结构的过程并非没有错误的开端和误入歧途,但目前呈现出的图景是,不同丝的旋转对称性存在多样性,且在静息肌肉中肌球蛋白头部的组织方式有一定程度的共性。一些剩余的差异可能与肌肉的调节方式有关。心肌肌球蛋白丝中的几种蛋白质可携带与心脏病相关的突变,因此阐明肌球蛋白丝结构以了解这些突变的影响具有明确且热门的临床意义。