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

C Shu, G Yi, T Watts, CC Kao, P Li - Nature structural & molecular …, 2012 - nature.com
C Shu, G Yi, T Watts, CC Kao, P Li
Nature structural & molecular biology, 2012nature.com
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.
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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