Computational redesign of protein-protein interaction specificity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2004-04

AUTHORS

Tanja Kortemme, Lukasz A Joachimiak, Alex N Bullock, Aaron D Schuler, Barry L Stoddard, David Baker

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. More... »

PAGES

371-379

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsmb749

DOI

http://dx.doi.org/10.1038/nsmb749

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1000957972

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/15034550


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