Stimulator of interferon genes: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The <scene name='57/573101/Cv/5'>U-shaped cleft</scene> between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A Tyr residue from each monomer stacks against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>. | The 3D structure of the complex between human STING and cyclic GMP-AMP shows the dinucleotide bound by the symmetric dimer of STING. The <scene name='57/573101/Cv/5'>U-shaped cleft</scene> between the 2 subunits makes numerous interactions with the U-shaped ligand. <scene name='57/573101/Cv/4'>GMP-AMP binding site</scene> (water molecules are shown as red spheres). A <scene name='57/573101/Cv/6'>Tyr residue from each monomer stacks</scene> against each of the purine moieties while an Arg residue from each monomer forms hydrogen bonds to the dinucleotide <ref>PMID:23910378</ref>. | ||
</StructureSection> | </StructureSection> | ||