Open AccessCrystallization studies of the murine c‐di‐GMP sensor protein STING
Author(s) -
Su YiChe,
Tu ZhiLe,
Yang ChaoYu,
Chin KoHsin,
Chuah Mary LayCheng,
Liang ZhaoXun,
Chou ShanHo
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112024372
Subject(s) - sting , stimulator of interferon genes , irf3 , innate immune system , cytosol , interferon , regulator , microbiology and biotechnology , tank binding kinase 1 , chemistry , biology , transcription factor , gene , kinase , biochemistry , protein kinase a , receptor , genetics , mitogen activated protein kinase kinase , engineering , enzyme , aerospace engineering
The innate immune response is the first defence system against pathogenic microorganisms, and cytosolic detection of pathogen‐derived DNA is believed to be one of the major mechanisms of interferon production. Recently, the mammalian ER membrane protein STING ( st imulator of I F N g enes; also known as MITA, ERIS, MPYS and TMEM173) has been found to be the master regulator linking the detection of cytosolic DNA to TANK‐binding kinase 1 (TBK1) and its downstream transcription factor IFN regulatory factor 3 (IRF3). In addition, STING itself was soon discovered to be a direct sensor of bacterial cyclic dinucleotides such as c‐di‐GMP or c‐di‐AMP. However, structural studies of apo STING and its complexes with these cyclic dinucleotides and with other cognate binding proteins are essential in order to fully understand the roles played by STING in these crucial signalling pathways. In this manuscript, the successful crystallization of the C‐terminal domain of murine STING (STING‐CTD; residues 138–344) is reported. Native and SeMet‐labelled crystals were obtained and diffracted to moderate resolutions of 2.39 and 2.2 Å, respectively.