Ontology highlight
ABSTRACT:
SUBMITTER: Dagliyan O
PROVIDER: S-EPMC3637791 | biostudies-literature | 2013 Apr
REPOSITORIES: biostudies-literature
Dagliyan Onur O Shirvanyants David D Karginov Andrei V AV Ding Feng F Fee Lanette L Chandrasekaran Srinivas N SN Freisinger Christina M CM Smolen Gromoslaw A GA Huttenlocher Anna A Hahn Klaus M KM Dokholyan Nikolay V NV
Proceedings of the National Academy of Sciences of the United States of America 20130408 17
Design of a regulatable multistate protein is a challenge for protein engineering. Here we design a protein with a unique topology, called uniRapR, whose conformation is controlled by the binding of a small molecule. We confirm switching and control ability of uniRapR in silico, in vitro, and in vivo. As a proof of concept, uniRapR is used as an artificial regulatory domain to control activity of kinases. By activating Src kinase using uniRapR in single cells and whole organism, we observe two u ...[more]