Solution structure of the N-terminal domain of DC-UbP/UBTD2 and its interaction with ubiquitin

被引：7

作者：

Song, Ai-Xin ^{[1
]}

Zhou, Chen-Jie ^{[1
]}

Guan, Xiao ^{[2
,3
]}

Sze, Kong-Hung ^{[2
,3
]}

Hu, Hong-Yu ^{[1
]}

机构：

[1] Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol, State Key Lab Mol Biol, Shanghai 200031, Peoples R China

[2] Univ Hong Kong, Dept Chem, Hong Kong, Hong Kong, Peoples R China

[3] Univ Hong Kong, Inst Mol Technol Drug Discovery & Synth, Open Lab Chem Biol, Hong Kong, Hong Kong, Peoples R China

来源：

PROTEIN SCIENCE | 2010年 / 19卷 / 05期

基金：

美国国家科学基金会;

关键词：

DC-UbP/UBTD2; solution structure; ubiquitin-binding domain; ubiquitin-like domain; NMR; BINDING DOMAINS; DENDRITIC CELLS; CHEMICAL-SHIFT; UBA DOMAINS; SH3; DOMAINS; DC-UBP; PROTEIN; NMR; IDENTIFICATION; RECOGNITION;

D O I：

10.1002/pro.386

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

DC-UbP/UBTD2 is a ubiquitin (Ub) domain-containing protein first identified from dendritic cells, and is implicated in ubiquitination pathway. The solution structure and backbone dynamics of the C-terminal Ub-like (UbL) domain were elucidated in our previous work. To further understand the biological function of DC-UbP, we then solved the solution structure of the N-terminal domain of DC-UbP (DC-UbP_N) and studied its Ub binding properties by NMR techniques. The results show that DC-UbP_N holds a novel structural fold and acts as a Ub-binding domain (UBD) but with low affinity. This implies that the DC-UbP protein, composing of a combination of both UbL and UBD domains, might play an important role in regulating protein ubiquitination and delivery of ubiquitinated substrates in eukaryotic cells.

引用

页码：1104 / 1109

页数：6

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