Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2
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Human uracil N-glycosylase isoform 2—UNG2 consists of an N-terminal intrinsically disordered regulatory domain (UNG2 residues 1–92, 9.3 kDa) and a C-terminal structured catalytic domain (UNG2 residues 93–313, 25.1 kDa). Here, we report the backbone 1H, 13C, and 15N chemical shift assignment as well as secondary structure analysis of the N-and C-terminal domains of UNG2 representing the full-length UNG2 protein.
KeywordsUracil-DNA glycosylase Uracil N-glycosylase isoform 2 UNG2 DNA repair Intrinsically disordered domain
Sequence- and ligation independent cloning
Uracil N-glycosylase isoform 2
Residues 1–92 of UNG2
Proliferating cell nuclear antigen
Replication protein A
Chitin binding domain
Residues 93–313 of UNG2-G93C
This work was financed by the MARPOL project, the Norwegian NMR Platform and a FRINAT project, all from the Research Council of Norway (Grant Numbers 221576, 226244, and 221538, respectively).
Compliance with ethical standards
Conflict of interest
The authors declare that they have no conflict of interest.
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