Improving mass spectrometry analysis of protein structures with arginine-selective chemical cross-linkers

doi:10.1038/s41467-019-11917-z

	Improving mass spectrometry analysis of protein structures with arginine-selective chemical cross-linkers
	Jones, Alexander X.1,2; Cao, Yong 3,4; Tangi, Yu-Liang 1,2; Wang, Jian-Hua 4; Ding, Yue-He 4; Tan, Hui 1,2; Chen, Zhen-Lin 5,6; Fang, Run-Qian 5,6; Yin, Jili 5,6; Chen, Rong-Chang 6,7; Zhu, Xing 6,7; She, Yang 4; Huang, Niu 4; Shao, Feng 4; Ye, Keqiong 6,7; Sun, Rui-Xiang 4; He, Si-Min 5,6; Lei, Xiaoguang 1,2; Dong, Meng-Qiu 4,8
	2019-09-02
发表期刊	NATURE COMMUNICATIONS
ISSN	2041-1723
卷号	10 页码:11
摘要	Chemical cross-linking of proteins coupled with mass spectrometry analysis (CXMS) is widely used to study protein-protein interactions (PPI), protein structures, and even protein dynamics. However, structural information provided by CXMS is still limited, partly because most CXMS experiments use lysine-lysine (K-K) cross-linkers. Although superb in selectivity and reactivity, they are ineffective for lysine deficient regions. Herein, we develop aromatic glyoxal cross-linkers (ArGOs) for arginine-arginine (R-R) cross-linking and the lysine-arginine (K-R) cross-linker KArGO. The R-R or K-R cross-links generated by ArGO or KArGO fit well with protein crystal structures and provide information not attainable by K-K cross-links. KArGO, in particular, is highly valuable for CXMS, with robust performance on a variety of samples including a kinase and two multi-protein complexes. In the case of the CNGP complex, KArGO cross-links covered as much of the PPI interface as R-R and K-K cross-links combined and improved the accuracy of Rosetta docking substantially.
DOI	10.1038/s41467-019-11917-z
收录类别	SCI
语种	英语
资助项目	National Key Research and Development Program of China[2017YFA0505200] ; Ministry of Science and Technology of China Projects 973[2015CB856200] ; Ministry of Science and Technology of China Projects 973[2014CB849800] ; Ministry of Science and Technology of China Projects 973[2013CB911203] ; National Natural Science Foundation of China[21625201] ; National Natural Science Foundation of China[21661140001] ; National Natural Science Foundation of China[91853202] ; National Natural Science Foundation of China[21521003] ; National Natural Science Foundation of China[21375010] ; municipal government of Beijing ; TIMBR ; Tsinghua University
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:000483305400002
出版者	NATURE PUBLISHING GROUP
引用统计	被引频次：42[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://119.78.100.204/handle/2XEOYT63/4778
专题	中国科学院计算技术研究所期刊论文_英文
通讯作者	Lei, Xiaoguang; Dong, Meng-Qiu
作者单位	1.Peking Univ, Beijing Natl Lab Mol Sci, Key Lab Bioorgan Chem & Mol Engn, Minist Educ,Dept Chem Biol,Coll Chem & Mol Engn,S, Beijing 100871, Peoples R China 2.Peking Univ, Peking Tsinghua Ctr Life Sci, Beijing 100871, Peoples R China 3.Peking Univ, Sch Life Sci, Beijing 100871, Peoples R China 4.Natl Inst Biol Sci, Beijing 102206, Peoples R China 5.Chinese Acad Sci, Inst Comp Technol, Key Lab Intelligent Informat Proc, Beijing 100049, Peoples R China 6.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 7.Chinese Acad Sci, CAS Ctr Excellence Biomacromol, Inst Biophys, Key Lab RNA Biol, Beijing 100101, Peoples R China 8.Tsinghua Univ, Tsinghua Inst Multidisciplinary Biomed Res, Beijing 102206, Peoples R China
推荐引用方式 GB/T 7714	Jones, Alexander X.,Cao, Yong,Tangi, Yu-Liang,et al. Improving mass spectrometry analysis of protein structures with arginine-selective chemical cross-linkers[J]. NATURE COMMUNICATIONS,2019,10:11.
APA	Jones, Alexander X..,Cao, Yong.,Tangi, Yu-Liang.,Wang, Jian-Hua.,Ding, Yue-He.,...&Dong, Meng-Qiu.(2019).Improving mass spectrometry analysis of protein structures with arginine-selective chemical cross-linkers.NATURE COMMUNICATIONS,10,11.
MLA	Jones, Alexander X.,et al."Improving mass spectrometry analysis of protein structures with arginine-selective chemical cross-linkers".NATURE COMMUNICATIONS 10(2019):11.