Hitchcock-DeGregori Sarah E
Department of Neuroscience and Cell Biology, Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, New Jersey 08854, USA.
Adv Exp Med Biol. 2008;644:60-72. doi: 10.1007/978-0-387-85766-4_5.
Tropomyosin is known as the archetypal coiled coil, being the first to be sequenced and modeled. Studies of the structure and dynamics of tropomyosin, accompanied by biochemical and biophysical analyses of tropomyosin, mutants and model peptides, have revealed the complexity and subtleties required for tropomyosin function. Interruptions in the canonical coiled coil allow for bends and regions of local instability that are required for tropomyosin to bind to the helical actin filament. This chapter highlights insights gained from recent structural studies as they relate to variations in tropomyosin's coiled-coil structure that are essential for binding to actin and the relationship of periodic repeats to actin molecules in the filament.
原肌球蛋白被认为是典型的卷曲螺旋，是首个被测序和建模的。对原肌球蛋白结构和动力学的研究，以及对原肌球蛋白、突变体和模型肽的生化和生物物理分析，揭示了原肌球蛋白发挥功能所需的复杂性和微妙之处。典型卷曲螺旋中的中断允许出现弯曲和局部不稳定区域，这是原肌球蛋白与螺旋状肌动蛋白丝结合所必需的。本章重点介绍了近期结构研究获得的见解，这些见解涉及原肌球蛋白卷曲螺旋结构的变化（这些变化对于与肌动蛋白结合至关重要）以及周期性重复序列与丝中肌动蛋白分子的关系。
