Article
Structural snapshots of base excision by the cancer-associated variant MutY N146S reveal a retaining mechanism.
Nucleic acids research - 22 Feb 2023
Demir Merve, Russelburg L Peyton, Lin Wen-Jen, Trasviña-Arenas Carlos H, Huang Beili, Yuen Philip K, Horvath Martin P, David Sheila S
Abstract excerpt
DNA glycosylase MutY plays a critical role in suppression of mutations resulted from oxidative damage, as highlighted by cancer-association of the human enzyme. MutY requires a highly conserved catalytic Asp residue for excision of adenines misinserted opposite 8-oxo-7,8-dihydroguanine (OG). A nearby Asn residue hydrogen bonds to the catalytic Asp in structures of MutY and its mutation to Ser is an inherited...
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