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.
Department of Biochemistry and Biophysics, Texas A&M University, College Station, Texas, USA.
Chang
C
Shu
Guanghui
G
Yi
Tylan
T
Watts
C Cheng
CC
Kao
Pingwei
P
Li
D000818:Animals; D002460:Cell Line; D006152:Cyclic GMP / Q000031:analogs & derivatives* / Q000378:metabolism; D006801:Humans; D006860:Hydrogen Bonding; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation; D000099197:STING Protein
D006152:Cyclic GMP; D008565:Membrane Proteins; C532857:STING1 protein, human; D000099197:STING Protein; C530855:Sting1 protein, mouse; C062025:bis(3',5')-cyclic diguanylic acid