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Noncatalytic Domains in DNA Glycosylases

Many proteins consist of two or more structural domains: separate parts that have a defined structure and function. For example, in enzymes, the catalytic activity is often localized in a core fragment, while other domains or disordered parts of the same protein participate in a number of regulatory...

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Detalles Bibliográficos
Autores principales: Torgasheva, Natalia A., Diatlova, Evgeniia A., Grin, Inga R., Endutkin, Anton V., Mechetin, Grigory V., Vokhtantsev, Ivan P., Yudkina, Anna V., Zharkov, Dmitry O.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9266487/
https://www.ncbi.nlm.nih.gov/pubmed/35806289
http://dx.doi.org/10.3390/ijms23137286
Descripción
Sumario:Many proteins consist of two or more structural domains: separate parts that have a defined structure and function. For example, in enzymes, the catalytic activity is often localized in a core fragment, while other domains or disordered parts of the same protein participate in a number of regulatory processes. This situation is often observed in many DNA glycosylases, the proteins that remove damaged nucleobases thus initiating base excision DNA repair. This review covers the present knowledge about the functions and evolution of such noncatalytic parts in DNA glycosylases, mostly concerned with the human enzymes but also considering some unique members of this group coming from plants and prokaryotes.