PROTEIN-KINASE-C ACTIVATION BY PHORBOL ESTERS - DO CYSTEINE-RICH REGIONS AND PSEUDOSUBSTRATE MOTIFS PLAY A ROLE

被引：122
|
作者：
GSCHWENDT, M
KITTSTEIN, W
MARKS, F
机构：
[1] M. Gschwendt, W. Kittstein and F. Marks are, the German Cancer Research Center, D-6900 Heidelberg
来源：
TRENDS IN BIOCHEMICAL SCIENCES | 1991年 / 16卷 / 05期
关键词：
D O I：
10.1016/0968-0004(91)90064-3
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
A model for the binding of two activators of protein kinase C (PKC), the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) and diacylglycerol, to the enzyme is proposed. It is suggested that each activator is hydrogen-bonded to sulfhydryl groups of cysteine residues and to the carbonyl of an asparagine within the cysteine-rich regions of PKC. This might induce a conformational change that would disrupt the association of the inhibitory pseudosubstrate sequence with the active center of PKC.
引用
收藏
页码：167 / 169
页数：3
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