Crystallization studies of the murine c-di-GMP sensor protein STING
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 (stimulator of IFN genes; also known as...
| Main Authors: | , , , , , , |
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| Other Authors: | |
| Format: | Journal Article |
| Language: | English |
| Published: |
2013
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| Online Access: | https://hdl.handle.net/10356/95453 http://hdl.handle.net/10220/9184 |
| _version_ | 1811697056954187776 |
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| author | Chou, Shan-Ho Su, Yi-Che Tu, Zhi-Le Yang, Chao-Yu Chin, Ko-Hsin Chuah, Mary Lay-Cheng Liang, Zhao-Xun |
| author2 | School of Biological Sciences |
| author_facet | School of Biological Sciences Chou, Shan-Ho Su, Yi-Che Tu, Zhi-Le Yang, Chao-Yu Chin, Ko-Hsin Chuah, Mary Lay-Cheng Liang, Zhao-Xun |
| author_sort | Chou, Shan-Ho |
| collection | NTU |
| description | 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 (stimulator of IFN genes; 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. |
| first_indexed | 2024-10-01T07:49:12Z |
| format | Journal Article |
| id | ntu-10356/95453 |
| institution | Nanyang Technological University |
| language | English |
| last_indexed | 2024-10-01T07:49:12Z |
| publishDate | 2013 |
| record_format | dspace |
| spelling | ntu-10356/954532023-02-28T17:03:35Z Crystallization studies of the murine c-di-GMP sensor protein STING Chou, Shan-Ho Su, Yi-Che Tu, Zhi-Le Yang, Chao-Yu Chin, Ko-Hsin Chuah, Mary Lay-Cheng Liang, Zhao-Xun School of Biological Sciences 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 (stimulator of IFN genes; 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. Published version 2013-02-20T03:45:19Z 2019-12-06T19:15:12Z 2013-02-20T03:45:19Z 2019-12-06T19:15:12Z 2012 2012 Journal Article Su, Y.- C., Tu, Z.- L., Yang, C.- Y., Chin, K.- H., Chuah, M. L.- C., Liang, Z.- X., et al. (2012). Crystallization studies of the murine c-di-GMP sensor protein STING. Acta Crystallographica Section F Structural Biology and Crystallization Communications, 68(8), 906-910. 1744-3091 https://hdl.handle.net/10356/95453 http://hdl.handle.net/10220/9184 10.1107/S1744309112024372 22869119 en Acta Crystallographica Section F Structural Biology and Crystallization Communications © 2012 International Union of Crystallography. This paper was published in Acta Crystallographica Section F Structural Biology and Crystallization Communications and is made available as an electronic reprint (preprint) with permission of International Union of Crystallography. The paper can be found at the following official DOI: [http://dx.doi.org/10.1107/S1744309112024372]. One print or electronic copy may be made for personal use only. Systematic or multiple reproduction, distribution to multiple locations via electronic or other means, duplication of any material in this paper for a fee or for commercial purposes, or modification of the content of the paper is prohibited and is subject to penalties under law. application/pdf |
| spellingShingle | Chou, Shan-Ho Su, Yi-Che Tu, Zhi-Le Yang, Chao-Yu Chin, Ko-Hsin Chuah, Mary Lay-Cheng Liang, Zhao-Xun Crystallization studies of the murine c-di-GMP sensor protein STING |
| title | Crystallization studies of the murine c-di-GMP sensor protein STING |
| title_full | Crystallization studies of the murine c-di-GMP sensor protein STING |
| title_fullStr | Crystallization studies of the murine c-di-GMP sensor protein STING |
| title_full_unstemmed | Crystallization studies of the murine c-di-GMP sensor protein STING |
| title_short | Crystallization studies of the murine c-di-GMP sensor protein STING |
| title_sort | crystallization studies of the murine c di gmp sensor protein sting |
| url | https://hdl.handle.net/10356/95453 http://hdl.handle.net/10220/9184 |
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