STRUCTURAL HOMOLOGIES AMONG MOTOR PROTEINS

传统的肌动蛋白和肌球蛋白是两个 负责运动性的不同的蛋白质超家族。而当 这两个蛋白质家族的成员都能产生力量并负责 为了产生运动，它们没有显示出可检测到的序列同源性， 尽管它们的三维结构显然是 相关的。我们已经确定了两者的同源区域 蛋白质的结构比较。这揭示了一种保守的 与其他ATPase共享的结构体系结构，并揭示了 肌动蛋白和肌球蛋白之间的残基保守。我们目前正在 检查这些残基以了解它们的功能。我们也是 将保守的结构区域与其他电机进行比较，在 特别是动力蛋白，也在寻找这个折叠的新成员 通过搜索序列数据库获得了一个新的家族。

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.