Flashman E, Korkie L, Watkins H, Redwood C, Moolman-Smook J C
The Department of Cardiovascular Medicine, University of Oxford, Oxford, UK.
FEBS Lett. 2008 Feb 6;582(3):434-8. doi: 10.1016/j.febslet.2008.01.004. Epub 2008 Jan 15.
Myosin-binding protein C (MyBPC) is proposed to take on a trimeric collar arrangement around the thick filament backbone in cardiac muscle, based on interactions between cardiac MyBPC domains C5 and C8. We have now determined, using yeast two-hybrid and in vitro binding assays, that the C5:C8 interaction is not dependent on the 28-residue cardiac-specific insert in C5. Furthermore, an interaction of similar affinity occurs between domains C5 and C8 of fast skeletal muscle MyBPC, but not between these domains of the slow skeletal muscle protein. These data have implications for the role and quaternary structure of MyBPC in skeletal muscle.
基于心肌肌球蛋白结合蛋白C（MyBPC）的C5和C8结构域之间的相互作用，有人提出它在心肌粗肌丝主干周围呈三聚体环状排列。我们现在通过酵母双杂交和体外结合试验确定，C5:C8相互作用不依赖于C5中28个氨基酸的心脏特异性插入序列。此外，快速骨骼肌MyBPC的C5和C8结构域之间也发生了具有相似亲和力的相互作用，但慢骨骼肌蛋白的这些结构域之间没有这种相互作用。这些数据对MyBPC在骨骼肌中的作用和四级结构具有重要意义。
