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• W2149792099 startingPage "8947" @default.
• W2149792099 abstract "Significance The presence of cytosolic DNA in mammalian cells signifies microbial invasions and triggers the DNA sensor protein cGAS to produce the second messenger molecule 2′3′-cGAMP, which elicits innate immune responses by binding to and activating the homodimerized adaptor protein STING. Here we show that the high affinity of the asymmetric ligand 2′3′-cGAMP to the symmetric dimer of STING originates from its unique mixed phosphodiester linkages. 2′3′-cGAMP, but not its linkage isomers, adopts an organized free-ligand conformation that resembles the STING-bound conformation and pays low energy costs in changing into the active conformation. Whereas biological structural studies have focused on analyses of protein conformations, our results demonstrate that analyses of free-ligand conformations can be equally important in understanding protein–ligand interactions." @default.
• W2149792099 created "2016-06-24" @default.
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• W2149792099 date "2015-07-06" @default.
• W2149792099 modified "2023-09-25" @default.
• W2149792099 title "Molecular basis for the specific recognition of the metazoan cyclic GMP-AMP by the innate immune adaptor protein STING" @default.
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• W2149792099 doi "https://doi.org/10.1073/pnas.1507317112" @default.
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