Engineering metal-binding sites in proteins
Engineering metal-binding sites in proteins
复制标题
DOI：
10.1016/s0959-440x(97)80112-1
复制
发表时间：
1997-08-01
影响因子：
6.8
通讯作者：
Valentine, JS
中科院分区：
文献类型：
--
作者：
Lu, Y;Valentine, JS
金属结合位点已经被工程化到从头设计和天然存在的蛋白质中。尽管对天然蛋白质中现有金属结合位点的重新设计仍然为成功的设计提供了最大的希望，但在从头设计的蛋白质和肽中工程化金属结合位点的更具挑战性的目标正在以越来越高的频率实现。在天然存在的蛋白质中创建新的金属结合位点结合了这两种方法的优势。目前，这三种方法都被有效地用于阐明天然存在的金属蛋白的结构和功能。
Metal-binding sites have been engineered into both de novo designed and naturally occurring proteins. Although the redesign of existing metal-binding sites in naturally occurring proteins still offers the most promise for a successful design, the more challenging goal of engineering metal-binding sites in de novo designed proteins and peptides is being achieved with increasing frequency. Creating new metal-binding sites in naturally occurring proteins combines the strength of both approaches. Currently, all three approaches are being used effectively in elucidating the structure and function of naturally occurring metalloproteins.