Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2
Journal article, Peer reviewed
MetadataShow full item record
Original versionBiomolecular NMR Assignments. 2017, 1-8. 10.1007/s12104-017-9772-5
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.