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Synthesis and characterization of the first cysteine-rich domain of novel protein kinase C

✍ Scribed by Yoshiaki Yanai; Kazuhiro Irie; Hajime Ohigashi; Paul A. Wender

Publisher: Elsevier Science
Year: 1997
Tongue: English
Weight: 318 KB
Volume: 7
Category: Article
ISSN: 0960-894X
DOI: 10.1016/s0960-894x(96)00587-2

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✦ Synopsis

The first cysteine-rich domains (CRD's) of mouse PKCq and PKC/~ (~I-CRDI and 6-CRD1) were prepared by automated solid phase peptide synthesis. In the presence of phosphatidylsenne, zinc-folded ~I-CRD 1 did not bind [-SH]phorlx)l 12,13-dibutyrate (PDBu) at all while the zinc-folded second CRD of mouse PKG1 (q-CRD2) bound PDBu strongly with a Kd of 0.91 nM. Moreover, 6-CRD1 showed very weak PDBu binding affinity (Kd = ca.500 nM) while the Kdof the second CRD of mouse PKC6 was reported to be 1.9 nM. These results suggest that the second CRD's of PKCrl and PKC6 play an important role in the PDBu binding.

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