Buchinger Edith, Wiik Siv Å, Kusnierczyk Anna, Rabe Renana, Aas Per A, Kavli Bodil, Slupphaug Geir, Aachmann Finn L
NOBIPOL, Department of Biotechnology, NTNU-Norwegian University of Science and Technology, 7491, Trondheim, Norway.
Department of Nutrition, Institute of Basic Medical Sciences, University of Oslo, 0317, Oslo, Norway.
Biomol NMR Assign. 2018 Apr;12(1):15-22. doi: 10.1007/s12104-017-9772-5. Epub 2017 Sep 6.
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 H, C, and N chemical shift assignment as well as secondary structure analysis of the N-and C-terminal domains of UNG2 representing the full-length UNG2 protein.
人尿嘧啶N-糖基化酶同工型2（UNG2）由一个N端内在无序的调节结构域（UNG2第1至92位残基，9.3 kDa）和一个C端结构化催化结构域（UNG2第93至313位残基，25.1 kDa）组成。在此，我们报告了代表全长UNG2蛋白的UNG2 N端和C端结构域的主链H、C和N化学位移归属以及二级结构分析。
