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Cyclic GMP-AMP containing mixed phosphodiester linkages is an endogenous high-affinity ligand for STING.

Abstract：

:The presence of microbial or self DNA in the cytoplasm of mammalian cells is a danger signal detected by the DNA sensor cyclic-GMP-AMP (cGAMP) synthase (cGAS), which catalyzes the production of cGAMP that in turn serves as a second messenger to activate innate immune responses. Here we show that endogenous cGAMP in mammalian cells contains two distinct phosphodiester linkages, one between 2'-OH of GMP and 5'-phosphate of AMP, and the other between 3'-OH of AMP and 5'-phosphate of GMP. This molecule, termed 2'3'-cGAMP, is unique in that it binds to the adaptor protein STING with a much greater affinity than cGAMP molecules containing other combinations of phosphodiester linkages. The crystal structure of STING bound to 2'3'-cGAMP revealed the structural basis of this high-affinity binding and a ligand-induced conformational change in STING that may underlie its activation.

journal_name

Mol Cell

journal_title

Molecular cell

authors

Zhang X,Shi H,Wu J,Zhang X,Sun L,Chen C,Chen ZJ

doi

10.1016/j.molcel.2013.05.022

subject

Has Abstract

pub_date

2013-07-25 00:00:00

pages

226-35

issue

2

eissn

1097-2765

issn

1097-4164

pii

S1097-2765(13)00409-7

journal_volume

51

pub_type

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