探戈需要两个：外周蛋白的第二个膜结合位点

IF 4.4 2区生物学 Q2 BIOCHEMISTRY & MOLECULAR BIOLOGY Structure Pub Date : 2025-01-02 DOI:10.1016/j.str.2024.12.007

Anand Srivastavava

引用次数: 0

摘要

在本期《结构》杂志中，Soteriou等人利用细胞生物学、体外重构方法和分子动力学（MD）模拟来表征AKT1的膜关联。作者表明，AKT1 pleckstrin同源结构域包含两个必不可少的协同PI(3,4,5) p3结合位点，使AKT1在有效的下游信号传递所需的必要方向上稳定的膜结合。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

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

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)P₃-binding sites that enable stable membrane binding of AKT1 in the requisite orientation required for effective downstream signaling.

求助全文

通过发布文献求助，成功后即可免费获取论文全文。去求助

来源期刊

Structure 生物-生化与分子生物学

CiteScore

8.90

自引率

1.80%

发文量

155

审稿时长

3-8 weeks

期刊介绍： Structure aims to publish papers of exceptional interest in the field of structural biology. The journal strives to be essential reading for structural biologists, as well as biologists and biochemists that are interested in macromolecular structure and function. Structure strongly encourages the submission of manuscripts that present structural and molecular insights into biological function and mechanism. Other reports that address fundamental questions in structural biology, such as structure-based examinations of protein evolution, folding, and/or design, will also be considered. We will consider the application of any method, experimental or computational, at high or low resolution, to conduct structural investigations, as long as the method is appropriate for the biological, functional, and mechanistic question(s) being addressed. Likewise, reports describing single-molecule analysis of biological mechanisms are welcome. In general, the editors encourage submission of experimental structural studies that are enriched by an analysis of structure-activity relationships and will not consider studies that solely report structural information unless the structure or analysis is of exceptional and broad interest. Studies reporting only homology models, de novo models, or molecular dynamics simulations are also discouraged unless the models are informed by or validated by novel experimental data; rationalization of a large body of existing experimental evidence and making testable predictions based on a model or simulation is often not considered sufficient.