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


ABSTRACT: 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.

SUBMITTER: Smola M 

PROVIDER: S-EPMC6718146 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature

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

Smola Miroslav M   Birkus Gabriel G   Boura Evzen E  

Acta crystallographica. Section F, Structural biology communications 20190828 Pt 9


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 pre  ...[more]

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