Crystal structures of porcine STING(CBD)-CDN complexes reveal the mechanism of ligand recognition and discrimination of STING proteins
文献类型： 外文期刊
作者： Cong, Xiaoyan 1 ; Yuan, Zenglin 1 ; Du, Yijun 2 ; Wu, Bo 3 ; Lu, Defen 1 ; Wu, Xiangju 2 ; Zhang, Youjia 3 ; Li, Feng 4 ; We 1 ;
作者机构： 1.Shandong Univ, State Key Lab Microbial Technol, Jinan 250100, Shandong, Peoples R China
2.Shandong Acad Agr Sci, Inst Anim Sci & Vet Med, Shandong Key Lab Anim Dis Control & Breeding, Sangyuan Rd 8, Jinan 250100, Shandong, Peoples R China
3.Chinese Acad Sci, Hefei Inst Phys Sci, Magnet Field Lab, Key Lab High Magnet Field & Ion Beam Phys Biol, Hefei 230026, Anhui, Peoples R China
4.South Dakota State Univ, Dept Biol & Microbiol, Dept Vet & Biomed Sci, Brookings, SD 57007 USA
5.Shandong Asia Pacific Highharve Organisms Sci & T, 1 Jinneng Rd, Qihe 251100, Shandong, Peoples R China
关键词： signaling; pathogen-associated molecular pattern (PAMP); pattern recognition receptor (PRR); cyclic diadenosine monophosphate (c-di-AMP); interferon
期刊名称：JOURNAL OF BIOLOGICAL CHEMISTRY （ 影响因子：5.157； 五年影响因子：5.041 ）
ISSN：
年卷期： 2019 年 294 卷 30 期
页码：
收录情况： SCI
摘要： The cyclic dinucleotide (CDN)-stimulator of interferon genes (STING) pathway plays an important role in the detection of viral and bacterial pathogens in animals. Previous studies have shown that the metazoan second messenger cyclic [G(2 ',5 ')pA(3 ',5 ')p] (2 ',3 '-cGAMP) generated by cyclic GMP-AMP synthase cGAS binds STING with high affinity compared with bacterial CDNs such as c-di-GMP, c-di-AMP, and 3 ',3 '-cGAMP. Despite recent progress indicating that the CDN-binding domain (CBD) of dimeric STING binds asymmetric 2 ',3 '-cGAMP preferentially over symmetric 3 ',3 '-CDNs, it remains an open question whether STING molecules, such as human STING, adopt a symmetric dimeric conformation to efficiently engage its asymmetric ligand. Here, structural studies of the CBD from porcine STING (STING(CBD)) in complex with CDNs at 1.76-2.6 angstrom resolution revealed that porcine STING(CBD), unlike its human and mouse counterparts, can adopt an asymmetric ligand-binding pocket to accommodate the CDNs. We observed that the extensive interactions and shape complementarity between asymmetric 2 ',3 '-cGAMP and the ligand-binding pocket make it the most preferred ligand for porcine STING and that geometry constraints limit the binding between symmetric 3 ',3 '-CDN and porcine STING. The ligand-discrimination mechanism of porcine STING observed here expands our understanding of how the CDN-STING pathway is activated and of its role in antiviral defense.
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