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No magnesium is needed for binding of the stimulator of interferon genes to cyclic dinucleotides.
Acta Crystallographica Section F ( IF 0.968 ) Pub Date : 2019-08-28 , DOI: 10.1107/s2053230x19010999
Miroslav Smola,Gabriel Birkus,Evzen Boura

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.
更新日期:2019-11-01

 

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