Lin Y, Kishi H, Nakamura A, Takagi T, Kohama K
Department of Pharmacology, Gunma University School of Medicine, Japan.
Biochem Biophys Res Commun. 1998 Aug 28;249(3):656-9. doi: 10.1006/bbrc.1998.9000.
Talin, an actin-binding protein from smooth muscle, is shown to bind to myosin in such a way that it stimulates the ATPase activity of myosin irrespective of the phosphorylation state of myosin. The binding site is shown to be localized at the N-terminal, 47 KDa fragment. The position of the actin-binding site at the C terminal suggests that talin may work as a crosslinker between myosin and actin.
踝蛋白是一种来自平滑肌的肌动蛋白结合蛋白，研究表明它以一种方式与肌球蛋白结合，即无论肌球蛋白的磷酸化状态如何，它都会刺激肌球蛋白的ATP酶活性。结合位点显示位于N端47 kDa片段。肌动蛋白结合位点在C端的位置表明踝蛋白可能作为肌球蛋白和肌动蛋白之间的交联剂发挥作用。
