Kirchhausen T, Scarmato P, Harrison S C, Monroe J J, Chow E P, Mattaliano R J, Ramachandran K L, Smart J E, Ahn A H, Brosius J
Science. 1987 Apr 17;236(4799):320-4. doi: 10.1126/science.3563513.
The clathrin light chains fall into two major classes, LCA and LCB. In an intact clathrin triskelion, one light chain, of either class, is bound to the proximal segment of a heavy chain leg. Analysis of rat brain and liver complementary DNA clones for LCA and LCB shows that the two light chain classes are closely related. There appear to be several members of each class having deletions of varying length aligned at the same position. A set of ten heptad elements, characteristic of alpha-helical coiled coils, is a striking feature of the central part of each derived amino acid sequence. These observations suggest a model in which the alpha-helical segment mediates binding to clathrin heavy chains and the amino- and carboxyl-terminal segments mediate interactions with other proteins. They also suggest an explanation for the observed tissue-dependent size variation for members of each class.
网格蛋白轻链分为两大类，即LCA和LCB。在完整的网格蛋白三脚复合体中，两类中的任何一类的一条轻链都与重链臂的近端部分相连。对大鼠脑和肝中LCA和LCB的互补DNA克隆进行分析表明，这两类轻链密切相关。每一类似乎都有几个成员，它们在相同位置存在不同长度的缺失。一组十个七肽元件是每个推导氨基酸序列中心部分的显著特征，这些元件是α-螺旋卷曲螺旋所特有的。这些观察结果提示了一个模型，其中α-螺旋段介导与网格蛋白重链的结合，而氨基末端和羧基末端段介导与其他蛋白质的相互作用。它们还为观察到的每一类成员的组织依赖性大小变异提供了解释。
