4emu | pdb_00004emu
From Proteopedia
Crystal structure of ligand free human STING
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Structural highlights
Publication Abstract from PubMedSTING (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. Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system.,Shu C, Yi G, Watts T, Kao CC, Li P Nat Struct Mol Biol. 2012 Jun 24;19(7):722-4. doi: 10.1038/nsmb.2331. PMID:22728658[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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