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No magnesium is needed for binding of the stimulator of interferon genes to cyclic dinucleotides

M. Smola, G. Birkus, E. Boura,

. 2019 ; 75 (Pt 9) : 593-598. [pub] 20190828

Language English Country United States

Document type Journal Article

Grant support
RVO:61388963 Akademie Věd České Republiky

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PubMed Central from 2014 to 1 year ago
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Stimulator of interferon genes (STING) binds cyclic dinucleotides (CDNs), which induce a large conformational change of the protein. The structural basis of activation of STING by CDNs is rather well understood. Unliganded STING forms an open dimer that undergoes a large conformational change (∼10 Å) to a closed conformation upon the binding of a CDN molecule. This event activates downstream effectors of STING and subsequently leads to activation of the type 1 interferon response. However, a previously solved structure of STING with 3',3'-c-di-GMP shows Mg atoms mediating the interaction of STING with this CDN. Here, it is shown that no Mg atoms are needed for this interaction; in fact, magnesium can in some cases obstruct the binding of a CDN to STING.

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