Ontology highlight
ABSTRACT:
SUBMITTER: Chen C
PROVIDER: S-EPMC5442603 | biostudies-literature | 2017 May
REPOSITORIES: biostudies-literature
Chen Catherine C Nimlamool Wutigri W Miller Chad J CJ Lou Hua Jane HJ Turk Benjamin E BE
ACS chemical biology 20170329 5
Eukaryotic protein kinases typically phosphorylate substrates in the context of specific sequence motifs, contributing to specificity essential for accurate signal transmission. Protein kinases recognize their target sequences through complementary interactions within the active site cleft. As a step toward the construction of orthogonal kinase signaling systems, we have re-engineered the protein kinase Pim1 to alter its phosphorylation consensus sequence. Residues in the Pim1 catalytic domain i ...[more]