Article
Structure of human MUTYH and functional profiling of cancer-associated variants reveal an allosteric network between its [4Fe-4S] cluster cofactor and active site required for DNA repair.
Nature communications - 16 Apr 2025
Trasviña-Arenas Carlos H, Dissanayake Upeksha C, Tamayo Nikole, Hashemian Mohammad, Lin W Jonathan, Demir Merve, Hoyos-Gonzalez Nallely, Fisher Andrew J, Cisneros G Andrés, Horvath Martin P, David Sheila S
Abstract excerpt
MUTYH is a clinically important DNA glycosylase that thwarts mutations by initiating base-excision repair at 8-oxoguanine (OG):A lesions. The roles for its [4Fe-4S] cofactor in DNA repair remain enigmatic. Functional profiling of cancer-associated variants near the [4Fe-4S] cofactor reveals that most variations abrogate both retention of the cofactor and enzyme activity. Surprisingly, R241Q and N238S retained the...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.