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

Guijun Shang; Deyu Zhu; Ning Li; Junbing Zhang; Chunyuan Zhu; Defen Lu; Cuilan Liu; Qian Yu; Yanyu Zhao; Sujuan Xu; Lichuan Gu

doi:10.1038/nsmb.2332

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

Guijun Shang
, Deyu Zhu
, Ning Li
, Junbing Zhang
, Chunyuan Zhu
, Defen Lu
, Cuilan Liu
, Qian Yu
, Yanyu Zhao
, Sujuan Xu
, Lichuan Gu^*

^*此作品的通讯作者

Shandong University

科研成果: 期刊稿件 › 文章 › 同行评审

223 引用（Scopus）

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.

源语言	英语
页（从-至）	725-727
页数	3
期刊	Nature Structural and Molecular Biology
卷	19
期	7
DOI	https://doi.org/10.1038/nsmb.2332
出版状态	已出版 - 7月 2012
已对外发布	是

访问文件

10.1038/nsmb.2332

其它文件与链接

链接到 Scopus 的出版物

引用此

@article{76ecd3f1af0d4edea208af7fc43011be,

title = "Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP",

abstract = "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.",

author = "Guijun Shang and Deyu Zhu and Ning Li and Junbing Zhang and Chunyuan Zhu and Defen Lu and Cuilan Liu and Qian Yu and Yanyu Zhao and Sujuan Xu and Lichuan Gu",

year = "2012",

month = jul,

doi = "10.1038/nsmb.2332",

language = "英语",

volume = "19",

pages = "725--727",

journal = "Nature Structural and Molecular Biology",

issn = "1545-9993",

publisher = "Nature Research",

number = "7",

}

TY - JOUR

T1 - Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP

AU - Shang, Guijun

AU - Zhu, Deyu

AU - Li, Ning

AU - Zhang, Junbing

AU - Zhu, Chunyuan

AU - Lu, Defen

AU - Liu, Cuilan

AU - Yu, Qian

AU - Zhao, Yanyu

AU - Xu, Sujuan

AU - Gu, Lichuan

PY - 2012/7

Y1 - 2012/7

N2 - 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.

AB - 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.

UR - https://www.scopus.com/pages/publications/84863717085

U2 - 10.1038/nsmb.2332

DO - 10.1038/nsmb.2332

M3 - 文章

C2 - 22728660

AN - SCOPUS:84863717085

SN - 1545-9993

VL - 19

SP - 725

EP - 727

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

IS - 7

ER -

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

摘要

访问文件

其它文件与链接

指纹

引用此