Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2
Buchinger, Edith; Wiik, Siv Åshild; Kusnierczyk, Anna; Rabe, Renana; Aas, Per Arne; Kavli, Bodil Merete; Slupphaug, Geir; Aachmann, Finn Lillelund
Journal article, Peer reviewed
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Date
2017Metadata
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Abstract
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.