6S86

Human wtSTING in complex with 3'3'-c-di-GMP

Replaces:  6RM0

Summary for 6S86

• Entry DOI: 10.2210/pdb6s86/pdb
• Descriptor: Stimulator of Interferon genes, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one) (3 entities in total)
• Functional Keywords: activator, membrane protein, immune system, receptor, protein binding
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 47068.54

Authors

Smola, M.,Boura, E. (deposition date: 2019-07-08, release date: 2019-07-17, Last modification date: 2024-01-24)

Primary citation

Smola, M.,Birkus, G.,Boura, E.
No magnesium is needed for binding of the stimulator of interferon genes to cyclic dinucleotides.
Acta Crystallogr.,Sect.F, 75:593-598, 2019

PubMed 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.

PubMed: 31475926
DOI: 10.1107/S2053230X19010999

Experimental method

X-RAY DIFFRACTION (2.6 Å)