期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 70, 期 1, 页码 208-217出版社
WILEY
DOI: 10.1002/prot.21587
关键词
structural bioinformatics; structural genomics; molecular modeling; structure prediction; protein function
Metal ions are crucial for protein function. They participate in enzyme catalysis play regulatory roles, and help maintain protein structure. Current tools for predicting metal-protein interactions are based on proteins crystallized with their metal ions present (holo forms). However, a majoi of resolved structures are free of metal ions (apo forms). Moreover, metal binding is a dynamic process often involving conformational rearrangement of the binding pocket. Thus, effective predictions need to be based on the structure Of the apo state. Here. we report an approach that identifies transition metal-binding sites in apo forms with a resulting selectivity >95%. Applying the approach to apo forms in the Protein Data Bank and structural genomics initiative identifies a large number of previously unknown, putative metal-binding sites, and their amino acid residues, in some cases providing a first clue to the function of the protein.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据