Rad23A Inhibitors

Rad23A inhibitors are a class of chemical compounds designed to target and inhibit the function of Rad23A, a protein involved in DNA repair and protein degradation pathways. Rad23A plays a critical role in the nucleotide excision repair (NER) mechanism, where it helps recognize and repair damaged DNA by interacting with other repair proteins. Additionally, Rad23A is involved in the ubiquitin-proteasome system (UPS), where it functions as a ubiquitin receptor that helps shuttle polyubiquitinated proteins to the proteasome for degradation. By inhibiting Rad23A, these compounds can interfere with both the repair of damaged DNA and the regulated degradation of proteins, making Rad23A a central player in maintaining cellular homeostasis.

Chemically, Rad23A inhibitors are designed to target specific domains of the protein, such as its ubiquitin-associated (UBA) domains or ubiquitin-like (UBL) domain. These domains are essential for Rad23A's interactions with polyubiquitinated proteins and other components of the DNA repair and degradation machinery. Inhibitors may act by binding to these domains, preventing Rad23A from performing its role in substrate recognition or protein-protein interactions. Structure-based drug design and high-throughput screening are typically used to identify and optimize inhibitors that selectively target Rad23A without affecting related proteins. By inhibiting Rad23A, researchers can study its involvement in DNA repair processes, protein degradation pathways, and how its inhibition affects cellular responses to DNA damage and protein turnover. These inhibitors serve as valuable tools for understanding the molecular mechanisms of Rad23A in regulating genomic stability and protein quality control within the cell.