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Updated: May 21, 2026

Capture Compound Mass Spectrometry - A Powerful Tool to Identify Novel c-di-GMP Effector Proteins
Published on: March 29, 2015
Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP
Guijun Shang1, Deyu Zhu, Ning Li
1State Key Laboratory of Microbial Technology, School of Life Science, Shandong University, Jinan, China.
Abstract:
STING functions as both an adaptor protein signaling cytoplasmic double-stranded DNA and a direct immunosensor of cyclic diguanylate monophosphate (c-di-GMP). The crystal structures of the C-terminal domain of human STING (STING(CTD)) and its complex with c-di-GMP reveal how STING recognizes c-di-GMP. In response to c-di-GMP binding, two surface loops, which serve as a gate and latch of the cleft formed by the dimeric STING(CTD), undergo rearrangements to interact with the ligand.
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