Cargando…
The Role of Active-Site Residues Phe98, His239, and Arg243 in DNA Binding and in the Catalysis of Human Uracil–DNA Glycosylase SMUG1
Human SMUG1 (hSMUG1) hydrolyzes the N-glycosidic bond of uracil and some uracil lesions formed in the course of epigenetic regulation. Despite the functional importance of hSMUG1 in the DNA repair pathway, the damage recognition mechanism has been elusive to date. In the present study, our objective...
Autores principales: | Iakovlev, Danila A., Alekseeva, Irina V., Vorobjev, Yury N., Kuznetsov, Nikita A., Fedorova, Olga S. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6749576/ https://www.ncbi.nlm.nih.gov/pubmed/31466351 http://dx.doi.org/10.3390/molecules24173133 |
Ejemplares similares
-
Uracil–DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms
por: Pettersen, Henrik Sahlin, et al.
Publicado: (2007) -
Excision of uracil from DNA by hSMUG1 includes strand incision and processing
por: Alexeeva, Marina, et al.
Publicado: (2019) -
Thermodynamics of the DNA Damage Repair Steps of Human 8-Oxoguanine DNA Glycosylase
por: Kuznetsov, Nikita A., et al.
Publicado: (2014) -
Structure of the uracil complex of Vaccinia virus uracil DNA glycosylase
por: Schormann, N., et al.
Publicado: (2013) -
A unique uracil-DNA binding protein of the uracil DNA glycosylase superfamily
por: Sang, Pau Biak, et al.
Publicado: (2015)