| First Author | Shu C | Year | 2012 |
| Journal | Nat Struct Mol Biol | Volume | 19 |
| Issue | 7 | Pages | 722-4 |
| PubMed ID | 22728658 | Mgi Jnum | J:245392 |
| Mgi Id | MGI:5919660 | Doi | 10.1038/nsmb.2331 |
| Citation | Shu C, et al. (2012) Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system. Nat Struct Mol Biol 19(7):722-4 |
| abstractText | 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. |
