It takes two to tango: The second membrane-binding site in peripheral proteins

被引：0

作者：

Srivastavava, Anand ^{[1
]}

机构：

[1] Indian Inst Sci, Mol Biophys Unit, Bangalore 560012, Karnataka, India

来源：

STRUCTURE | 2025年 / 33卷 / 01期

基金：

英国惠康基金;

关键词：

MOLECULAR-MECHANISM;

D O I：

10.1016/j.str.2024.12.007

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：

In this issue of Structure, Soteriou et al.(1) use cell biology, in vitro reconstitution approaches, and molecular dynamics (MD) simulations to characterize the membrane association of AKT1. The authors show that the AKT1 pleckstrin homology domain contains two essential and cooperative PI(3,4,5)P-3-binding sites that enable stable membrane binding of AKT1 in the requisite orientation required for effective downstream signaling.

引用

页码：10 / 12

页数：3

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