MULTIDOMAIN METALLOPROTEINS

与核酸相互作用有关的一系列蛋白质 被发现包含围绕其组织的小结构域 结合的锌离子。这些领域中最具特点的是 Cys2His为2个“锌指”结构域。这些区域在多达1000个人类中出现 这些区域内的基因产物和突变被认为与 癌症的发展。通过结构和其他研究，它已经成为 可能基于以下因素设计合理的位点特异性DNA结合蛋白 这些域。将进行更多的研究以测试和推广 这些设计能力。此外，这种蛋白质的一些成员 家族被卷入对锌敏感的监管过程。金属 将进行结合研究，以测试锌指的作用 锌敏感中的结构域。其他蛋白质似乎是这一分子的成员 家族参与了RNA的剪接。金属结合与结构研究 将启动探索与DNA相互作用的作用最近 在神经系统表达的蛋白质中被发现。金属装订 并将进行结构研究，以阐明 这些结构域的特性使它们能够与DNA相互作用。已被占用 综上所述，这些研究将扩大我们对结构和 锌结合区在核酸和基因中的功能作用 调节蛋白。

A range of proteins implicated in interactions with nucleic acids have been found to contain small structural domains that are organized around bound zinc ions. The most well characterized of these domains are the Cys2His2 "zinc finger" domains. These domains occur in up to 1000 human gene products and mutations within these domains have been implicated in cancer development. Through structural and other studies, it has become possible to design rationally site-specific DNA binding proteins based on these domains. Additional studies will be performed to test and extend these design capabilities. In addition, some members of this protein family have been implicated in zinc sensitive regulatory processes. Metal binding studies will be performed to test the role of the zinc finger domains in zinc sensing. Other proteins that appear to be members of this family are involved in RNA splicing. Metal binding and structural studies will be initiated to probe the role of interactions with DNA has recently been discovered in proteins expressed in the nervous system. Metal binding and structural studies will be performed to elucidate the properties the properties of these domains that enable them to interact with DNA. Taken together, these studies will extend our knowledge of the structural and functional roles of zinc binding domains in nucleic acid and gene regulatory proteins.