Probing conformational hotspots for the recognition and intervention of protein complexes by lysine reactivity profiling.
Chem Sci
; 12(4): 1451-1457, 2020 Nov 23.
Article
in English
| MEDLINE | ID: covidwho-1387501
ABSTRACT
Probing the conformational and functional hotspot sites within aqueous native protein complexes is still a challenging task. Herein, a mass spectrometry (MS)-based two-step isotope labeling-lysine reactivity profiling (TILLRP) strategy is developed to quantify the reactivities of lysine residues and probe the molecular details of protein-protein interactions as well as evaluate the conformational interventions by small-molecule active compounds. The hotspot lysine sites that are crucial to the SARS-CoV-2 S1-ACE2 combination could be successfully probed, such as S1 Lys417 and Lys444. Significant alteration of the reactivities of lysine residues at the interaction interface of S1-RBD Lys386-Lys462 was observed during the formation of complexes, which might be utilized as indicators for investigating the S1-ACE2 dynamic recognition and intervention at the molecular level in high throughput.
Full text:
Available
Collection:
International databases
Database:
MEDLINE
Type of study:
Experimental Studies
Language:
English
Journal:
Chem Sci
Year:
2020
Document Type:
Article
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