title: Synthesis of protein kinase Cdelta C1b domain by native chemical ligation methodology and characterization of its folding and ligand binding.
abstract: The C1b domain of protein kinase Cdelta (PKCdelta), 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.
authors: Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, 2-3-10 Kandasurugadai, Chiyoda-ku, Tokyo 101-0062, Japan.
authors: Nami
authors: N
authors: Ohashi
authors: Wataru
authors: W
authors: Nomura
authors: Mai
authors: M
authors: Kato
authors: Tetsuo
authors: T
authors: Narumi
authors: Nancy E
authors: NE
authors: Lewin
authors: Peter M
authors: PM
authors: Blumberg
authors: Hirokazu
authors: H
authors: Tamamura
mesh_terms: D002851:Chromatography, High Pressure Liquid; D002942:Circular Dichroism; D008024:Ligands; D010446:Peptide Fragments / Q000138:chemical synthesis; D011485:Protein Binding; D017510:Protein Folding; D051745:Protein Kinase C-delta / Q000138:chemical synthesis / Q000737:chemistry* / Q000378:metabolism; D017434:Protein Structure, Tertiary
chemical_list: D008024:Ligands; D010446:Peptide Fragments; D051745:Protein Kinase C-delta