Improving mass spectrometry analysis of protein structures with arginine-selective chemical cross-linkers
文献类型：期刊论文
| 作者 | Jones, Alexander X.6,7; Cao, Yong4,5; Tangi, Yu-Liang6,7; Wang, Jian-Hua4; Ding, Yue-He4; Tan, Hui6,7; Chen, Zhen-Lin2,3; Fang, Run-Qian2,3; Yin, Jili2,3; Chen, Rong-Chang2,8 |
| 刊名 | NATURE COMMUNICATIONS
 |
| 出版日期 | 2019-09-02 |
| 卷号 | 10页码:11 |
| ISSN号 | 2041-1723 |
| DOI | 10.1038/s41467-019-11917-z |
| 英文摘要 | 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. |
| 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 |
| 语种 | 英语 |
| 出版者 | NATURE PUBLISHING GROUP |
| WOS记录号 | WOS:000483305400002 |
| 源URL | [http://119.78.100.204/handle/2XEOYT63/4777]  |
| 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.Tsinghua Univ, Tsinghua Inst Multidisciplinary Biomed Res, Beijing 102206, Peoples R China 2.Univ Chinese Acad Sci, Beijing 100049, Peoples R China 3.Chinese Acad Sci, Inst Comp Technol, Key Lab Intelligent Informat Proc, Beijing 100049, Peoples R China 4.Natl Inst Biol Sci, Beijing 102206, Peoples R China 5.Peking Univ, Sch Life Sci, Beijing 100871, Peoples R China 6.Peking Univ, Peking Tsinghua Ctr Life Sci, Beijing 100871, Peoples R China 7.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 8.Chinese Acad Sci, CAS Ctr Excellence Biomacromol, Inst Biophys, Key Lab RNA Biol, Beijing 100101, 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. |
入库方式： OAI收割
来源：计算技术研究所
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