Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/95453
Title: Crystallization studies of the murine c-di-GMP sensor protein STING
Authors: Chou, Shan-Ho
Su, Yi-Che
Tu, Zhi-Le
Yang, Chao-Yu
Chin, Ko-Hsin
Chuah, Mary Lay-Cheng
Liang, Zhao-Xun
Issue Date: 2012
Source: 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.
Series/Report no.: Acta Crystallographica Section F Structural Biology and Crystallization Communications
Abstract: 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.
URI: https://hdl.handle.net/10356/95453
http://hdl.handle.net/10220/9184
ISSN: 1744-3091
DOI: 10.1107/S1744309112024372
Rights: © 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.
Fulltext Permission: open
Fulltext Availability: With Fulltext
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