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

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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Main Authors: Carlos H. Trasviña-Arenas, Upeksha C. Dissanayake, Nikole Tamayo, Mohammad Hashemian, Wen-Jen Lin, Merve Demir, Nallely Hoyos-Gonzalez, Andrew J. Fisher, G. Andrés Cisneros, Martin P. Horvath, Sheila S. David
Format: Article
Language:English
Published: Nature Portfolio 2025-04-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-025-58361-w
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https://doi.org/10.1038/s41467-025-58361-w

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