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