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

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.

authors

• Li, Pingwei

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

publisher

• Springer Nature  Publisher

published in

• Nature Structural and Molecular Biology  Journal

keywords

• Animals
• Cell Line
• Cyclic GMP
• Humans
• Hydrogen Bonding
• Membrane Proteins
• Mice
• Models, Molecular
• Protein Conformation

Digital Object Identifier (DOI)

• 10.1038/nsmb.2331

start page

• 722

end page

• 724

volume

• 19

issue

• 7

URL

• http%3A%2F%2Fdx.doi.org%2F10.1038%2Fnsmb.2331