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

Abstract 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...

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Váldodahkkit:	Carlos H. Trasviña-Arenas, Upeksha C. Dissanayake, Nikole Tamayo, Mohammad Hashemian, W. Jonathan Lin, Merve Demir, Nallely Hoyos-Gonzalez, Andrew J. Fisher, G. Andrés Cisneros, Martin P. Horvath, Sheila S. David
Materiálatiipa:	Artigo
Giella:	Inglês
Almmustuhtton:	Nature Portfolio 2025-04-01
Ráidu:	Nature Communications
Liŋkkat:	https://doi.org/10.1038/s41467-025-58361-w
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