STRUCTURAL HOMOLOGIES AMONG MOTOR PROTEINS

传统的驱动蛋白和肌球蛋白是两个 负责运动的蛋白质的不同超家族。 而 两个蛋白质家族的成员都产生力， 为了产生运动，它们没有显示出可检测的序列同源性， 尽管它们的三维结构明显 相关. 我们已经确定了这两个同源区域 蛋白质结构比较 这揭示了一种保守的 与其他ATP酶共享的结构架构，并揭示了 在驱动蛋白和肌球蛋白之间保守的残基。 我们目前正在 检查这些残留物以了解它们的功能。 我们也 将保守的结构区域与其他马达进行比较， 特别是动力蛋白，并寻找新的成员， 通过搜索序列数据库。

Conventional kinesin and myosin are founding members of two distinct superfamilies of proteins responsible for motility. While members of both protein families generate force and are responsible for producing motion, they show no detectable sequence homology, despite the fact that their three-dimensional structures are clearly related. We have determined the homologous regions of the two proteins by structural comparison. This has revealed a conserved structural architecture shared with other ATPases, and has revealed residues conserved between kinesin and myosin. We are currently examining these residues to understand their function. We are also comparing the conserved structural regions to other motors, in particular dynein, and also searching for novel members of this fold family by searching sequence databases.