Synthesis and phorbol ester-binding studies of the individual cysteine-rich motifs of protein kinase D

被引：16

作者：

Irie, K ^{[1
]}

Nakahara, A

Ohigashi, H

Fukuda, H

Wender, PA

Konishi, H

Kikkawa, U

机构：

[1] Kyoto Univ, Grad Sch Agr, Div Appl Life Sci, Kyoto 6068502, Japan

[2] PE Biosyst Japan Ltd, Minato Ku, Tokyo 1060032, Japan

[3] Stanford Univ, Dept Chem, Stanford, CA 94305 USA

[4] Kobe Univ, Biosignal Res Ctr, Kobe, Hyogo 6578501, Japan

来源：

BIOORGANIC & MEDICINAL CHEMISTRY LETTERS | 1999年 / 9卷 / 17期

关键词：

D O I：

10.1016/S0960-894X(99)00413-8

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

To investigate the phorbol ester-binding properties of the individual cysteine rich motifs of protein kinase D (PKD), the (52)-mer peptides containing each cysteine-rich motif of PKD (PKD-C1A, PKD-C1B) have been synthesized. The [H-3]phorbol-12,13-dibutyrate (PDBu) binding to PKD-C1A was affected drastically by incubation temperature while that to PKD-C1B was not. Scatchard analysis of [H-3]PDBu binding to both PKD C1 peptides gave dissociation constants of 2.5 +/- 0.4 and 2.7 +/- 0.8 nM for PKD-C1A and PKD-C1B, respectively, indicating that the two cysteine-rich motifs of PKD are functionally equivalent like those of PKC gamma. (C) 1999 Elsevier Science Ltd. All rights reserved.

引用

页码：2487 / 2490

页数：4

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