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

被引：0
|
作者：
Chang Shu
Guanghui Yi
Tylan Watts
C Cheng Kao
Pingwei Li
机构：
[1] Texas A&M University,Department of Biochemistry and Biophysics
[2] Indiana University,Department of Molecular and Cellular Biochemistry
来源：
Nature Structural & Molecular Biology | 2012年 / 19卷
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摘要：
The crystal structures of human STING in the apo and c-di-GMP–bound states, supported by mutagenesis and biochemical data, reveal that c-di-GMP binds to preformed dimeric STING. c-di-GMP prolongs STING phosphorylation in vitro, which may contribute to downstream IFN signaling. These findings aid in understanding the innate immune response to bacterial infection.
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页码：722 / 724
页数：2
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