| http://purl.uniprot.org/citations/30842659 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30842659 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30842659 | http://www.w3.org/2000/01/rdf-schema#comment | "Infections by pathogens that contain DNA trigger the production of type-I interferons and inflammatory cytokines through cyclic GMP-AMP synthase, which produces 2'3'-cyclic GMP-AMP (cGAMP) that binds to and activates stimulator of interferon genes (STING; also known as TMEM173, MITA, ERIS and MPYS)1-8. STING is an endoplasmic-reticulum membrane protein that contains four transmembrane helices followed by a cytoplasmic ligand-binding and signalling domain9-13. The cytoplasmic domain of STING forms a dimer, which undergoes a conformational change upon binding to cGAMP9,14. However, it remains unclear how this conformational change leads to STING activation. Here we present cryo-electron microscopy structures of full-length STING from human and chicken in the inactive dimeric state (about 80 kDa in size), as well as cGAMP-bound chicken STING in both the dimeric and tetrameric states. The structures show that the transmembrane and cytoplasmic regions interact to form an integrated, domain-swapped dimeric assembly. Closure of the ligand-binding domain, induced by cGAMP, leads to a 180° rotation of the ligand-binding domain relative to the transmembrane domain. This rotation is coupled to a conformational change in a loop on the side of the ligand-binding-domain dimer, which leads to the formation of the STING tetramer and higher-order oligomers through side-by-side packing. This model of STING oligomerization and activation is supported by our structure-based mutational analyses."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41586-019-0998-5"xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41586-019-0998-5"xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/author | "Chen Z.J."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/author | "Chen Z.J."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/author | "Zhang X."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/author | "Zhang X."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/author | "Zhang C."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/author | "Zhang C."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/author | "Shang G."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/author | "Shang G."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/author | "Bai X.C."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/author | "Bai X.C."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/name | "Nature"xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/pages | "389-393"xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/pages | "389-393"xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/title | "Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/title | "Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP."xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/volume | "567"xsd:string |
| http://purl.uniprot.org/citations/30842659 | http://purl.uniprot.org/core/volume | "567"xsd:string |