Identification of novel pleckstrin homology (PH) domains provides a hypothesis for PH domain function.

Identification of novel pleckstrin homology (PH) domains provides a hypothesis for PH domain function.
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新型 pleckstrin 同源 (PH) 结构域的鉴定为 PH 结构域功能提供了假设。

DOI:
10.1006/bbrc.1993.2164
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发表时间:
1993
影响因子:
3.1
通讯作者:
Shaw,G
Shaw,G
中科院分区:
生物学4区
文献类型:
--
作者:
Shaw,G

文献摘要

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普列克底物蛋白(Pleckstrin)同源结构域在蛋白质序列数据库中很难用计算机程序找到。为了克服这个困难,开发了一个简单的程序,鉴定出三种含有以前未被识别的PH结构域的蛋白质:β-肾上腺素能受体激酶(β-方舟)、thetecA蛋白激酶和胰岛素受体底物蛋白IRS-1。含有新PH结构域的β-方舟区域与先前显示的结合三聚体G蛋白的βγ亚基的区域一致,提示PH结构域功能的一般假设。PH结构域,然后发现在N-末端的tecA同源Btkanditk。与该假说一致,Btkis PH结构域的点突变与信号转导缺陷有关。
Pleckstrin homology (PH) domains are difficult to find in protein sequence databases with widely used computer programs. A simple program developed to overcome this difficulty identified three proteins containing previously unrecognized PH domains; the β-adrenergic receptor kinase (β-ARK), thetecAprotein kinase and the insulin receptor substrate protein IRS-1. The region of β-ARK containing the novel PH domain coincides with that previously shown to bind the βγ subunits of trimeric G-proteins, suggesting a general hypothesis for PH domain function. PH domains were then found at the N-termini of thetecAhomologuesBtkanditk. In line with the hypothesis a point mutation in the PH domain ofBtkis associated with defects in signal transduction.