4EMU

Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system.

(2012) Nat Struct Mol Biol 19: 722-724

• PubMed: 22728658 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1038/nsmb.2331
• Primary Citation of Related Structures:  
  4EMT, 4EMU


• PubMed Abstract: 
  

  STING (stimulator of interferon genes) is an innate immune sensor of cyclic dinucleotides that regulates the induction of type I interferons. STING's C-terminal domain forms a V-shaped dimer and binds a cyclic diguanylate monophosphate (c-di-GMP) at the dimer interface by both direct and solvent-mediated hydrogen bonds. Guanines of c-di-GMP stack against the phenolic rings of a conserved tyrosine, and mutations at the c-di-GMP binding surface reduce nucleotide binding and affect signaling.

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Organizational Affiliation: 

Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.