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Computational redesign of protein-protein interaction specificity.

Abstract：

: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.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Kortemme T,Joachimiak LA,Bullock AN,Schuler AD,Stoddard BL,Baker D

doi

10.1038/nsmb749

keywords:

subject

Has Abstract

pub_date

2004-04-01 00:00:00

pages

371-9

issue

4

eissn

1545-9993

issn

1545-9985

pii

nsmb749

journal_volume

11

pub_type

杂志文章

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