三联体蛋白：一类具有新型富含半胱氨酸特征的新蛋白质。
TRIADs: a new class of proteins with a novel cysteine-rich signature.
作者信息
van der Reijden B A, Erpelinck-Verschueren C A, Löwenberg B, Jansen J H
机构信息
Institute of Hematology, Erasmus University Rotterdam, The Netherlands.
出版信息
Protein Sci. 1999 Jul;8(7):1557-61. doi: 10.1110/ps.8.7.1557.
Abstract
Triad1 was recently identified as a nuclear RING finger protein, which is up-regulated during retinoic acid induced granulocytic differentiation of acute leukemia cells. Here we show that a cysteine-rich domain (C6HC), present in Triad1, is conserved in at least 24 proteins encoded by various eukaryotes. The C6HC consensus pattern C-x(4)-C-x(14-30)-C-x(1-4)-C-x(4)-C-x(2)-C-x(4)-H-x(4)-C defines this structure as the fourth family member of the zinc-binding RING, LIM, and LAP/PHD fingers. Strikingly, in 22 of 24 proteins the C6HC domain is flanked by two RING finger structures. We have termed the novel C6HC motif DRIL (double RING finger linked). The strong conservation of the larger tripartite TRIAD (two RING fingers and DRIL) structure indicates that the three subdomains are functionally linked and identifies a novel class of proteins.
摘要
Triad1最近被鉴定为一种核环指蛋白，在视黄酸诱导的急性白血病细胞粒细胞分化过程中上调。在此我们表明，Triad1中存在的富含半胱氨酸结构域（C6HC）在各种真核生物编码的至少24种蛋白质中是保守的。C6HC共有模式C-x(4)-C-x(14 - 30)-C-x(1 - 4)-C-x(4)-C-x(2)-C-x(4)-H-x(4)-C将该结构定义为锌结合环指、LIM和LAP/PHD指的第四个家族成员。引人注目的是，在24种蛋白质中的22种中，C6HC结构域两侧是两个环指结构。我们将这种新的C6HC基序称为DRIL（双环指连接）。更大的三联体（两个环指和DRIL）结构的高度保守表明这三个亚结构域在功能上是相连的，并确定了一类新的蛋白质。
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