Arf调节蛋白PH结构域的变构特性。

Cellular logistics Pub Date : 2016-04-26 eCollection Date: 2016-04-01 DOI:10.1080/21592799.2016.1181700
Neeladri Sekhar Roy, Marielle E Yohe, Paul A Randazzo, James M Gruschus
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引用次数: 13

摘要

Pleckstrin同源结构域(PH)结合磷脂和蛋白质。它们是许多酶的关键调控元件,包括鸟嘌呤核苷酸交换因子(GEFs)和ras -超家族鸟嘌呤核苷酸结合蛋白(如adp -核糖基化因子(Arfs))的gtpase激活蛋白(gap)。近年来的研究表明,许多PH结构域可以与一个以上的配体协同结合。在这里,我们讨论了2个adp核糖基化因子交换因子Grp1和Brag2的PH结构域依赖变构行为的分子基础,配体与Grp1和Arf gtpase激活蛋白ASAP1的PH结构域的协同结合,以及相关催化结构域活性的后果。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Allosteric properties of PH domains in Arf regulatory proteins.

Allosteric properties of PH domains in Arf regulatory proteins.

Allosteric properties of PH domains in Arf regulatory proteins.

Allosteric properties of PH domains in Arf regulatory proteins.

Pleckstrin Homology (PH) domains bind phospholipids and proteins. They are critical regulatory elements of a number enzymes including guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) for Ras-superfamily guanine nucleotide binding proteins such as ADP-ribosylation factors (Arfs). Recent studies have indicated that many PH domains may bind more than one ligand cooperatively. Here we discuss the molecular basis of PH domain-dependent allosteric behavior of 2 ADP-ribosylation factor exchange factors, Grp1 and Brag2, cooperative binding of ligands to the PH domains of Grp1 and the Arf GTPase-activating protein, ASAP1, and the consequences for activity of the associated catalytic domains.

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