期刊
BIOCHEMISTRY
卷 47, 期 51, 页码 13564-13572出版社
AMER CHEMICAL SOC
DOI: 10.1021/bi8017448
关键词
-
资金
- National Institutes of Health [GM 57571]
Coiled coils have long been recognized as the major constituent of many fibrous proteins and also serve as oligomerization domains in a wide variety of proteins. More recently, it has become clear that the surfaces of two-stranded coiled coils are also involved in macromolecular recognition. Indeed, the helical hairpin or intramolecular antiparallel coiled coil (ACC) can serve as a protein or nucleic acid recognition motif. Protein kinase N (PKN) interacts with the small GTPase RhoA through ACC motifs. The crystal structure of RhoA with the N-terminal ACC motif (PKN-ACC1) is unusual in that these proteins interact through two distinct surfaces. Using the ACC domain of seryl tRNA synthetase (SRS-ACC) as a scaffold for protein grafting experiments, we show that RhoA interacts with only one face of PKN-ACC1. This result highlights the potential of the SRS-ACC scaffold for protein engineering applications and provides insight into the mechanism of RhoA-mediated signal transduction through PKN.
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