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外周膜蛋白的动态结构形成。

Dynamic structure formation of peripheral membrane proteins.

机构信息

Cellular Biophysics Group, German Cancer Research Center, Heidelberg, Germany.

出版信息

PLoS Comput Biol. 2011 Jun;7(6):e1002067. doi: 10.1371/journal.pcbi.1002067. Epub 2011 Jun 23.

DOI:10.1371/journal.pcbi.1002067
PMID:21731477
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3121687/
Abstract

Using coarse-grained membrane simulations we show here that peripheral membrane proteins can form a multitude of higher-order structures due to membrane-mediated interactions. Peripheral membrane proteins characteristically perturb the lipid bilayer in their vicinity which supports the formation of protein assemblies not only within the same but surprisingly also across opposing leaflets of a bilayer. In addition, we also observed the formation of lipid-protein domains on heteregeneous membranes. The clustering ability of proteins, as quantified via the potential of mean force, is enhanced when radius and hydrophobic penetration depth of the proteins increases. Based on our data, we propose that membrane-mediated cluster formation of peripheral proteins supports protein assembly in vivo and hence may play a pivotal role in the formation of templates for signaling cascades and in the emergence of transport intermediates in the secretory pathway.

摘要

使用粗粒化膜模拟,我们在此展示了由于膜介导的相互作用,外周膜蛋白可以形成多种高级结构。外周膜蛋白的特征是在其附近扰动脂质双层,这支持了蛋白质组装的形成,不仅在同一层内,而且令人惊讶的是,也在双层的相对叶层之间。此外,我们还观察到在异质膜上形成脂质-蛋白质域。通过平均力势能定量蛋白质的聚类能力,当蛋白质的半径和疏水性穿透深度增加时,聚类能力会增强。基于我们的数据,我们提出了膜介导的外周蛋白簇形成支持了体内蛋白质组装,因此可能在信号级联模板的形成和分泌途径中运输中间体的出现中发挥关键作用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/502743b29ef0/pcbi.1002067.g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/ed1b4065471f/pcbi.1002067.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/96a2362e597b/pcbi.1002067.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/23e21b29fb66/pcbi.1002067.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/d58523af242f/pcbi.1002067.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/bbd3270983b6/pcbi.1002067.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/7c368da94b76/pcbi.1002067.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/68fc23c83476/pcbi.1002067.g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/502743b29ef0/pcbi.1002067.g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/ed1b4065471f/pcbi.1002067.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/96a2362e597b/pcbi.1002067.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/23e21b29fb66/pcbi.1002067.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/d58523af242f/pcbi.1002067.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/bbd3270983b6/pcbi.1002067.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/7c368da94b76/pcbi.1002067.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/68fc23c83476/pcbi.1002067.g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/5ea6/3121687/502743b29ef0/pcbi.1002067.g008.jpg

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