Berg J M, Shi Y
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Science. 1996 Feb 23;271(5252):1081-5. doi: 10.1126/science.271.5252.1081.
Zinc ions are key structural components of a large number of proteins. The binding of zinc stabilizes the folded conformations of domains so that they may facilitate interactions between the proteins and other macromolecules such as DNA. The modular nature of some of these zinc-containing proteins has allowed the rational design of site-specific DNA binding proteins. The ability of zinc to be bound specifically within a range of tetrahedral sites appears to be responsible for the evolution of the side range of zinc-stabilized structural domains now known to exist. The lack of redox activity for the zinc ion and its binding and exchange kinetics also may be important in the use of zinc for specific functional roles.
锌离子是大量蛋白质的关键结构成分。锌的结合稳定了结构域的折叠构象,从而有助于蛋白质与其他大分子(如DNA)之间的相互作用。其中一些含锌蛋白质的模块化性质使得能够合理设计位点特异性DNA结合蛋白。锌在一系列四面体位点内特异性结合的能力似乎是目前已知的锌稳定结构域广泛存在的进化原因。锌离子缺乏氧化还原活性及其结合和交换动力学在锌用于特定功能角色方面也可能很重要。