Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP

被引：197

作者：

Shang, Guijun ^{[1
]}

Zhu, Deyu ^{[1
]}

Li, Ning ^{[1
]}

Zhang, Junbing ^{[1
]}

Zhu, Chunyuan ^{[1
]}

Lu, Defen ^{[1
]}

Liu, Cuilan ^{[1
]}

Yu, Qian ^{[1
]}

Zhao, Yanyu ^{[1
]}

Xu, Sujuan ^{[1
]}

Gu, Lichuan ^{[1
]}

机构：

[1] Shandong Univ, Sch Life Sci, State Key Lab Microbial Technol, Jinan 250100, Peoples R China

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2012年 / 19卷 / 07期

关键词：

MPYS; TRANSDUCTION; DIGUANYLATE; RECEPTORS; ADAPTER; AMP;

D O I：

10.1038/nsmb.2332

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：

STING functions as both an adaptor protein signaling cytoplasmic double-stranded DNA and a direct immunosensor of cyclic diguanylate monophosphate (c-di-GMP). The crystal structures of the C-terminal domain of human STING (STING(CTD)) and its complex with c-di-GMP reveal how STING recognizes c-di-GMP. In response to c-di-GMP binding, two surface loops, which serve as a gate and latch of the cleft formed by the dimeric STING(CTD), undergo rearrangements to interact with the ligand.

引用

页码：725 / +

页数：4

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