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Synthesis of protein kinase Cδ C1b domain by native chemical ligation methodology and characterization of its folding and ligand binding
Author(s) -
Ohashi Nami,
Nomura Wataru,
Kato Mai,
Narumi Tetsuo,
Lewin Nancy E.,
Blumberg Peter M.,
Tamamura Hirokazu
Publication year - 2009
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1161
Subject(s) - diacylglycerol kinase , protein kinase c , chemistry , native chemical ligation , folding (dsp implementation) , ligand (biochemistry) , phosphorylation , biochemistry , biophysics , microbiology and biotechnology , computational biology , receptor , biology , chemical synthesis , in vitro , electrical engineering , engineering
The C1b domain of protein kinase Cδ (PKCδ), a potent receptor for ligands such as diacylglycerol and phorbol esters, was synthesized by utilizing native chemical ligation. With this synthetic strategy, the domain was efficiently constructed and shown to have high affinity ligand binding and correct folding. The C1b domain has been utilized for the development of novel ligands for the control of phosphorylation by PKC family members. This strategy will pave the way for the efficient construction of C1b domains modified with fluorescent dyes, biotin, etc. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd.