Computational redesign of protein-protein interaction specificity
Computational redesign of protein-protein interaction specificity
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DOI：
10.1038/nsmb749
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发表时间：
2004-04-01
影响因子：
16.8
通讯作者：
Baker, D
中科院分区：
文献类型：
--
作者：
Kortemme, T;Joachimiak, LA;Baker, D
We developed a computational second-site suppressor strategy to redesign specificity at a protein-protein interface and applied it to create new specifically interacting DNase-inhibitor protein pairs. We demonstrate that the designed switch in specificity holds in in vitro binding and functional assays. We also show that the designed interfaces are specific in the natural functional context in living cells, and present the first high-resolution X-ray crystallographic analysis of a computer-redesigned functional protein-protein interface with altered specificity. The approach should be applicable to the design of interacting protein pairs with novel specificities for delineating and re-engineering protein interaction networks in living cells.
