Synthesis of protein kinase Cdelta C1b domain by native chemical ligation methodology and characterization of its folding and ligand binding.
作者信息
Ohashi Nami, Nomura Wataru, Kato Mai, Narumi Tetsuo, Lewin Nancy E, Blumberg Peter M, Tamamura Hirokazu
机构信息
Institute of Biomaterials and Bioengineering, Tokyo Medical and Dental University, 2-3-10 Kandasurugadai, Chiyoda-ku, Tokyo 101-0062, Japan.
出版信息
J Pept Sci. 2009 Oct;15(10):642-6. doi: 10.1002/psc.1161.
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.
摘要
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