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Synthesis of protein kinase Cδ C1b domain by native chemical ligation methodology and characterization of its folding and ligand binding

2009; Wiley; Volume: 15; Issue: 10 Linguagem: Inglês

10.1002/psc.1161

1099-1387

Nami Ohashi, Wataru Nomura, Mai Kato, Tetsuo Narumi, Nancy E. Lewin, Peter M. Blumberg, Hirokazu Tamamura,

Receptor Mechanisms and Signaling

Abstract 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.