DICP OpenIR
Improving mass spectrometry analysis of protein structures with arginine-selective chemical cross-linkers
Jones, Alexander X.1,2; Cao, Yong3,4; Tangi, Yu-Liang1,2; Wang, Jian-Hua4; Ding, Yue-He4; Tan, Hui1,2; Chen, Zhen-Lin5,6; Fang, Run-Qian5,6; Yin, Jili5,6; Chen, Rong-Chang6,7; Zhu, Xing6,7; She, Yang4; Huang, Niu4; Shao, Feng4; Ye, Keqiong6,7; Sun, Rui-Xiang4; He, Si-Min5,6; Lei, Xiaoguang1,2; Dong, Meng-Qiu4,8
Corresponding AuthorLei, Xiaoguang(xglei@pku.edu.cn) ; Dong, Meng-Qiu(dongmengqiu@nibs.ac.cn)
Source PublicationNATURE COMMUNICATIONS
2019-09-02
ISSN2041-1723
DOI10.1038/s41467-019-11917-z
Volume10Pages:11
Funding ProjectNational 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
Funding OrganizationNational Key Research and Development Program of China ; National Key Research and Development Program of China ; Ministry of Science and Technology of China Projects 973 ; Ministry of Science and Technology of China Projects 973 ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; municipal government of Beijing ; municipal government of Beijing ; TIMBR ; TIMBR ; Tsinghua University ; Tsinghua University ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; Ministry of Science and Technology of China Projects 973 ; Ministry of Science and Technology of China Projects 973 ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; municipal government of Beijing ; municipal government of Beijing ; TIMBR ; TIMBR ; Tsinghua University ; Tsinghua University ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; Ministry of Science and Technology of China Projects 973 ; Ministry of Science and Technology of China Projects 973 ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; municipal government of Beijing ; municipal government of Beijing ; TIMBR ; TIMBR ; Tsinghua University ; Tsinghua University ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; Ministry of Science and Technology of China Projects 973 ; Ministry of Science and Technology of China Projects 973 ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; municipal government of Beijing ; municipal government of Beijing ; TIMBR ; TIMBR ; Tsinghua University ; Tsinghua University
WOS SubjectMultidisciplinary Sciences
WOS Research AreaScience & Technology - Other Topics
WOS KeywordACIDIC RESIDUES ; LINKING ; ARCHITECTURE ; REAGENTS ; RNA ; MS ; BIOCONJUGATION ; IDENTIFICATION ; TRACELESS ; PEPTIDES
AbstractChemical 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.
Language英语
Funding OrganizationNational Key Research and Development Program of China ; National Key Research and Development Program of China ; Ministry of Science and Technology of China Projects 973 ; Ministry of Science and Technology of China Projects 973 ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; municipal government of Beijing ; municipal government of Beijing ; TIMBR ; TIMBR ; Tsinghua University ; Tsinghua University ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; Ministry of Science and Technology of China Projects 973 ; Ministry of Science and Technology of China Projects 973 ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; municipal government of Beijing ; municipal government of Beijing ; TIMBR ; TIMBR ; Tsinghua University ; Tsinghua University ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; Ministry of Science and Technology of China Projects 973 ; Ministry of Science and Technology of China Projects 973 ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; municipal government of Beijing ; municipal government of Beijing ; TIMBR ; TIMBR ; Tsinghua University ; Tsinghua University ; National Key Research and Development Program of China ; National Key Research and Development Program of China ; Ministry of Science and Technology of China Projects 973 ; Ministry of Science and Technology of China Projects 973 ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; municipal government of Beijing ; municipal government of Beijing ; TIMBR ; TIMBR ; Tsinghua University ; Tsinghua University
WOS IDWOS:000483305400002
PublisherNATURE PUBLISHING GROUP
Citation statistics
Cited Times:2[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/173339
Collection中国科学院大连化学物理研究所
Corresponding AuthorLei, Xiaoguang; Dong, Meng-Qiu
Affiliation1.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
Recommended Citation
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.
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