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STING 与环二鸟苷酸结合的结构揭示了免疫系统识别环二核苷酸的机制。

Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system.

机构信息

Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.

出版信息

Nat Struct Mol Biol. 2012 Jun 24;19(7):722-4. doi: 10.1038/nsmb.2331.

DOI:10.1038/nsmb.2331
PMID:22728658
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3392545/
Abstract

STING (stimulator of interferon genes) is an innate immune sensor of cyclic dinucleotides that regulates the induction of type I interferons. STING's C-terminal domain forms a V-shaped dimer and binds a cyclic diguanylate monophosphate (c-di-GMP) at the dimer interface by both direct and solvent-mediated hydrogen bonds. Guanines of c-di-GMP stack against the phenolic rings of a conserved tyrosine, and mutations at the c-di-GMP binding surface reduce nucleotide binding and affect signaling.

摘要

STING(干扰素基因刺激物)是一种环二核苷酸的先天免疫传感器,可调节 I 型干扰素的诱导。STING 的 C 端结构域形成 V 形二聚体,并通过直接和溶剂介导的氢键在二聚体界面上结合环二鸟苷酸单磷酸(c-di-GMP)。c-di-GMP 的鸟嘌呤与保守的酪氨酸的酚环堆叠,而 c-di-GMP 结合表面的突变会降低核苷酸结合并影响信号转导。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e050/3392545/c8ffe382963f/nihms-379464-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e050/3392545/8c59b1d2d73d/nihms-379464-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e050/3392545/b17fbdb8019d/nihms-379464-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e050/3392545/c8ffe382963f/nihms-379464-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e050/3392545/8c59b1d2d73d/nihms-379464-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e050/3392545/b17fbdb8019d/nihms-379464-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/e050/3392545/c8ffe382963f/nihms-379464-f0003.jpg

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