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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-...

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Publisher copy:
10.1038/nsmb749

Authors


Kortemme, T More by this author
Joachimiak, LA More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Schuler, AD More by this author
Stoddard, BL More by this author
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Journal:
Nature structural and molecular biology
Volume:
11
Issue:
4
Pages:
371-379
Publication date:
2004-04-05
DOI:
EISSN:
1545-9985
ISSN:
1545-9993
URN:
uuid:ef7407ed-87ac-4765-b010-0f75d785ffda
Source identifiers:
92566
Local pid:
pubs:92566

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