Abstract：
: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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Jones AX,Cao Y,Tang YL,Wang JH,Ding YH,Tan H,Chen ZL,Fang RQ,Yin J,Chen RC,Zhu X,She Y,Huang N,Shao F,Ye K,Sun RX,He SM,Lei X,Dong MQdoi
10.1038/s41467-019-11917-zsubject
Has Abstractpub_date
2019-09-02 00:00:00pages
3911issue
1issn
2041-1723pii
10.1038/s41467-019-11917-zjournal_volume
10pub_type
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