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Novel c-di-GMP recognition modes of the mouse innate immune adaptor protein STING

หน่วยงาน Nanyang Technological University, Singapore

รายละเอียด

ชื่อเรื่อง : Novel c-di-GMP recognition modes of the mouse innate immune adaptor protein STING
นักวิจัย : Chin, Ko-Hsin , Tu, Zhi-Le , Su, Yi-Che , Yu, Yu-Jen , Chen, Hui-Chen , Lo, Yuan-Chao , Chen, Chin-Pan , Barber, Glen N. , Chuah, Mary Lay-Cheng , Liang, Zhao-Xun , Chou, Shan-Ho
คำค้น : DRNTU::Science::Biological sciences
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2556
อ้างอิง : Chin, K.-H., Tu, Z.-L., Su, Y.-C., Yu, Y.-J., Chen, H.-C., Lo, Y.-C., et al. (2013). Novel c-di-GMP recognition modes of the mouse innate immune adaptor protein STING. Acta Crystallographica Section D: Biological Crystallography, D69, 352-366. , 0907-4449 , http://hdl.handle.net/10220/10980 , http://dx.doi.org/10.1107/S0907444912047269
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : Acta crystallographica section D : biological crystallography
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

The mammalian ER protein STING (stimulator of interferon genes; also known as MITA, ERIS, MPYS or TMEM173) is an adaptor protein that links the detection of cytosolic dsDNA to the activation of TANK-binding kinase 1 (TBK1) and its downstream transcription factor interferon regulatory factor 3 (IFN3). Recently, STING itself has been found to be the direct receptor of bacterial c-di-GMP, and crystal structures of several human STING C-terminal domain (STING-CTD) dimers in the apo form or in complex with c-di-GMP have been published. Here, a novel set of structures of mouse STING-CTD (mSTING137-344) in apo and complex forms determined from crystals obtained under different crystallization conditions are reported. These novel closed-form structures exhibited considerable differences from previously reported open-form human STING-CTD structures. The novel mSTING structures feature extensive interactions between the two monomers, a unique asymmetric c-di-GMP molecule with one guanine base in an unusual syn conformation that is well accommodated in the dimeric interface with many direct specific interactions and two unexpected equivalent secondary peripheral c-di-GMP binding sites. Replacement of the amino acids crucial for specific c-di-GMP binding in mSTING significantly changes the ITC titration profiles and reduces the IFN-[beta] reporter luciferase activity. Taken together, these results reveal a more stable c-di-GMP binding mode of STING proteins that could serve as a template for rational drug design to stimulate interferon production by mammalian cells.

บรรณานุกรม :
Chin, Ko-Hsin , Tu, Zhi-Le , Su, Yi-Che , Yu, Yu-Jen , Chen, Hui-Chen , Lo, Yuan-Chao , Chen, Chin-Pan , Barber, Glen N. , Chuah, Mary Lay-Cheng , Liang, Zhao-Xun , Chou, Shan-Ho . (2556). Novel c-di-GMP recognition modes of the mouse innate immune adaptor protein STING.
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Chin, Ko-Hsin , Tu, Zhi-Le , Su, Yi-Che , Yu, Yu-Jen , Chen, Hui-Chen , Lo, Yuan-Chao , Chen, Chin-Pan , Barber, Glen N. , Chuah, Mary Lay-Cheng , Liang, Zhao-Xun , Chou, Shan-Ho . 2556. "Novel c-di-GMP recognition modes of the mouse innate immune adaptor protein STING".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Chin, Ko-Hsin , Tu, Zhi-Le , Su, Yi-Che , Yu, Yu-Jen , Chen, Hui-Chen , Lo, Yuan-Chao , Chen, Chin-Pan , Barber, Glen N. , Chuah, Mary Lay-Cheng , Liang, Zhao-Xun , Chou, Shan-Ho . "Novel c-di-GMP recognition modes of the mouse innate immune adaptor protein STING."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2556. Print.
Chin, Ko-Hsin , Tu, Zhi-Le , Su, Yi-Che , Yu, Yu-Jen , Chen, Hui-Chen , Lo, Yuan-Chao , Chen, Chin-Pan , Barber, Glen N. , Chuah, Mary Lay-Cheng , Liang, Zhao-Xun , Chou, Shan-Ho . Novel c-di-GMP recognition modes of the mouse innate immune adaptor protein STING. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2556.