Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2023 Jun 15;14:3564. doi: 10.1038/s41467-023-39268-w

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 8 — a Schematic cartoon illustrating the workflow of competitive MS-based ABPP experiment to determine protein targets of covalent ligands, as read out by the large LFQ (control/treated samples). Created using ChemDraw and MS Powerpoint. b The scout ligand, CL-Sc, shows binding onto 1177 cysteines probed by NAIA-5, i.e., these cysteines are ligandable. Among them, 616 are uniquely profiled by NAIA-5 and have not been found in the reported study of DBIA. c The number of probe-modified proteins being liganded by CL-Sc. d A liganded Cys591 on POLRMT is located close to the promoter-binding domain; PDB ID: 3SPA. e Left: A ligandable Cys392 on RAD21 is located at the interface of RAD21 and SA2. Right: zoom-in image showing Cys392 and other key residues at the binding interface of RAD21 and SA2. PDB ID: 4PJU.