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

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.

published proceedings

  • Nat Struct Mol Biol

altmetric score

  • 12.5

author list (cited authors)

  • Shu, C., Yi, G., Watts, T., Kao, C. C., & Li, P.

citation count

  • 209

complete list of authors

  • Shu, Chang||Yi, Guanghui||Watts, Tylan||Kao, C Cheng||Li, Pingwei

publication date

  • January 2012