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Updated: May 19, 2026
Capture Compound Mass Spectrometry - A Powerful Tool to Identify Novel c-di-GMP Effector Proteins
Published on: March 29, 2015
Crystallization studies of the murine c-di-GMP sensor protein STING
Yi-Che Su1, Zhi-Le Tu, Chao-Yu Yang
1Institute of Biochemistry, National Chung Hsing University, Taichung 40227, Taiwan.
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.
Insights
Researchers crystallized the C-terminal domain of stimulator of IFN genes (STING) protein. This structural study is essential for understanding STING
Area of Science:
- Immunology
- Structural Biology
- Biochemistry
Background:
- The innate immune system provides the first defense against pathogens.
- Cytosolic DNA detection is a key mechanism for interferon production.
- STING (stimulator of IFN genes) is a master regulator in the cytosolic DNA sensing pathway, linking DNA detection to TBK1 and IRF3 activation.
Purpose of the Study:
- To understand the structural basis of STING function in innate immunity.
- To facilitate further studies on STING's interaction with cyclic dinucleotides and other binding proteins.
- To enable detailed structural analysis of STING's role in interferon production.
Main Methods:
- Crystallization of the C-terminal domain of murine STING (STING-CTD).
- Obtained native and SeMet-labelled crystals.
- Diffraction analysis to moderate resolutions (2.39 and 2.2 Å).
Main Results:
- Successfully crystallized the STING-CTD.
- Achieved diffraction of native crystals to 2.39 Å.
- Achieved diffraction of SeMet-labelled crystals to 2.2 Å.
Conclusions:
- The crystallization of STING-CTD provides a foundation for detailed structural studies.
- This structural information is crucial for elucidating STING's mechanism of action in innate immune signaling.
- Further structural investigations will illuminate STING's role in sensing cyclic dinucleotides and mediating interferon responses.
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