A novel ADP- and zinc-binding fold from function-directed in vitro evolution
A novel ADP- and zinc-binding fold from function-directed in vitro evolution
复制标题
DOI：
10.1038/nsmb745
复制
发表时间：
2004-04-01
影响因子：
16.8
通讯作者：
Sollazzo, M
中科院分区：
文献类型：
--
作者：
Lo Surdo, P;Walsh, MA;Sollazzo, M
生物学家面临的一个巨大挑战是创造具有新折叠和定制功能的蛋白质。作为从头蛋白质设计的替代方案，我们研究了随机生成的靶向结合ATP的蛋白质的结构。晶体结构揭示了一种新的α/β折叠结合其配体，代表了第一个蛋白质结构来自体外进化和第一个核苷酸结合蛋白稳定的锌离子。
A great challenge to biologists is to create proteins with novel folds and tailored functions. As an alternative to de novo protein design, we investigated the structure of a randomly generated protein targeted to bind ATP. The crystal structure reveals a novel alpha/beta fold bound to its ligand, representing both the first protein structure derived from in vitro evolution and the first nucleotide-binding protein stabilized by a zinc ion.