Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2

被引：9

作者：

Buchinger, Edith ^{[1
]}

Wiik, Siv A. ^{[1
,3
]}

Kusnierczyk, Anna ^{[2
]}

Rabe, Renana ^{[2
]}

Aas, Per. A. ^{[2
]}

Kavli, Bodil ^{[2
]}

Slupphaug, Geir ^{[2
]}

Aachmann, Finn L. ^{[1
]}

机构：

[1] NTNU Norwegian Univ Sci & Technol, Dept Biotechnol, NOBIPOL, N-7491 Trondheim, Norway

[2] NTNU Norwegian Univ Sci & Technol, Dept Canc Res & Mol Med, N-7491 Trondheim, Norway

[3] Univ Oslo, Inst Basic Med Sci, Dept Nutr, N-0317 Oslo, Norway

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2018年 / 12卷 / 01期

关键词：

Uracil-DNA glycosylase; Uracil N-glycosylase isoform 2; UNG2; DNA repair; Intrinsically disordered domain; EXPRESSION LEVELS; STRUCTURAL BASIS; REPAIR; SPECIFICITY; PROTEINS; RPA;

D O I：

10.1007/s12104-017-9772-5

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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-1, C-13, and N-15 chemical shift assignment as well as secondary structure analysis of the N-and C-terminal domains of UNG2 representing the full-length UNG2 protein.

引用

页码：15 / 22

页数：8

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