Quantification of the transferability of a designed protein specificity switch reveals extensive epistasis in molecular recognition.
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ABSTRACT: Reengineering protein-protein recognition is an important route to dissecting and controlling complex interaction networks. Experimental approaches have used the strategy of "second-site suppressors," where a functional interaction is inferred between two proteins if a mutation in one protein can be compensated by a mutation in the second. Mimicking this strategy, computational design has been applied successfully to change protein recognition specificity by predicting such sets of compensatory mutations in protein-protein interfaces. To extend this approach, it would be advantageous to be able to "transplant" existing engineered and experimentally validated specificity changes to other homologous protein-protein complexes. Here, we test this strategy by designing a pair of mutations that
SUBMITTER: Melero C
PROVIDER: S-EPMC4217408 | biostudies-literature | 2014 Oct
REPOSITORIES: biostudies-literature
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