期刊
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
卷 23, 期 13, 页码 -出版社
MDPI
DOI: 10.3390/ijms23137286
关键词
DNA repair; base excision repair; DNA glycosylases; noncatalytic protein domains; intrinsically disordered protein regions; protein-protein interactions; post-translational modifications; DNA binding; lesion search in DNA
资金
- Russian Science Foundation [21-64-00017]
- Russian Ministry of Science and Education [121031300056-8]
This review provides current knowledge on the functions and evolution of noncatalytic parts in DNA glycosylases, focusing primarily on human enzymes but also considering unique members from plants and prokaryotes.
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.
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