4EMT

Crystal Structure of human STING bound to c-di-GMP

4EMT の概要

• エントリーDOI: 10.2210/pdb4emt/pdb
• 関連するPDBエントリー: 4EMU
• 分子名称: Transmembrane protein 173, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: alpha/beta fold, innate immune sensor, c-di-gmp, c-di-amp, membrane protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Endoplasmic reticulum membrane; Multi-pass membrane protein: Q86WV6
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 43966.38

構造登録者

Li, P. (登録日: 2012-04-12, 公開日: 2012-06-13, 最終更新日: 2024-11-06)

主引用文献

Shu, C.,Yi, G.,Watts, T.,Kao, C.C.,Li, P.
Structure of STING bound to cyclic di-GMP reveals the mechanism of cyclic dinucleotide recognition by the immune system.
Nat.Struct.Mol.Biol., 19:722-724, 2012

PubMed 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.

PubMed: 22728658
DOI: 10.1038/nsmb.2331

実験手法

X-RAY DIFFRACTION (1.5 Å)