期刊
JOURNAL OF PROTEOME RESEARCH
卷 6, 期 5, 页码 1833-1845出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr060674u
关键词
post-translational modifications; protein-protein interaction; surface accessibility; intrinsic disorder; domains and linkers
Protein post-translational modifications are crucial to the function of many proteins. In this study, we have investigated the structural environment of 8378 incidences of 44 types of post-translational modifications with 19 different approaches. We show that modified amino acids likely to be involved in protein-protein interactions, such as ester-linked phosphorylation, methylarginine, acetyllysine, sulfotyrosine, hydroxyproline, and hydroxylysine, are clearly surface associated. Other modifications, including O-GlcNAc, phosphohistidine, 4-aspartylphosphate, methyllysine, and ADP-ribosylarginine, are either not surface associated or are in a protein's core. Artifactual modifications were found to be randomly distributed throughout the protein. We discuss how the surface accessibility of post-translational modifications can be important for protein-protein interactivity. Keywords: post-translational modifications center dot protein-protein interaction center dot surface accessibility center dot intrinsic disorder center dot domains and linkers
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据