4F9E

Cyclic di-GMP Sensing via the Innate Immune Signaling Protein STING

4F9E の概要

• エントリーDOI: 10.2210/pdb4f9e/pdb
• 関連するPDBエントリー: 4F9G
• 分子名称: Transmembrane protein 173 (2 entities in total)
• 機能のキーワード: sting, eris, mita, stimulator of interferon genes protein, innate immunity 5helix and 5 beta strand, protein binding
• 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: 1
• 化学式量合計: 29848.46

構造登録者

Kabaleeswaran, V.,Wu, H. (登録日: 2012-05-18, 公開日: 2012-07-25, 最終更新日: 2024-02-28)

主引用文献

Yin, Q.,Tian, Y.,Kabaleeswaran, V.,Jiang, X.,Tu, D.,Eck, M.J.,Chen, Z.J.,Wu, H.
Cyclic di-GMP Sensing via the Innate Immune Signaling Protein STING.
Mol.Cell, 46:735-745, 2012

PubMed Abstract: Detection of foreign materials is the first step of successful immune responses. Stimulator of interferon genes (STING) was shown to directly bind cyclic diguanylate monophosphate (c-di-GMP), a bacterial second messenger, and to elicit strong interferon responses. Here we elucidate the structural features of the cytosolic c-di-GMP binding domain (CBD) of STING and its complex with c-di-GMP. The CBD exhibits an α + β fold and is a dimer in the crystal and in solution. Surprisingly, one c-di-GMP molecule binds to the central crevice of a STING dimer, using a series of stacking and hydrogen bonding interactions. We show that STING is autoinhibited by an intramolecular interaction between the CBD and the C-terminal tail (CTT) and that c-di-GMP releases STING from this autoinhibition by displacing the CTT. The structures provide a remarkable example of pathogen-host interactions in which a unique microbial molecule directly engages the innate immune system.

PubMed: 22705373
DOI: 10.1016/j.molcel.2012.05.029

実験手法

X-RAY DIFFRACTION (2.75 Å)