5BQX
Crystal structure of human STING in complex with 3'2'-cGAMP
Summary for 5BQX
| Entry DOI | 10.2210/pdb5bqx/pdb |
| Related | 4KSY |
| Descriptor | Stimulator of interferon genes protein, 3'2'-cGAMP (3 entities in total) |
| Functional Keywords | sting, 3'2'-cgamp, immune system |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 27855.06 |
| Authors | Wu, J.,Zhang, X.,Chen, Z.J.,Chen, C. (deposition date: 2015-05-29, release date: 2015-06-24, Last modification date: 2024-03-06) |
| Primary citation | Shi, H.,Wu, J.,Chen, Z.J.,Chen, C. Molecular basis for the specific recognition of the metazoan cyclic GMP-AMP by the innate immune adaptor protein STING. Proc.Natl.Acad.Sci.USA, 112:8947-8952, 2015 Cited by PubMed Abstract: Cyclic GMP-AMP containing a unique combination of mixed phosphodiester linkages (2'3'-cGAMP) is an endogenous second messenger molecule that activates the type-I IFN pathway upon binding to the homodimer of the adaptor protein STING on the surface of endoplasmic reticulum membrane. However, the preferential binding of the asymmetric ligand 2'3'-cGAMP to the symmetric dimer of STING represents a physicochemical enigma. Here we show that 2'3'-cGAMP, but not its linkage isomers, adopts an organized free-ligand conformation that resembles the STING-bound conformation and pays low entropy and enthalpy costs in converting into the active conformation. Our results demonstrate that analyses of free-ligand conformations can be as important as analyses of protein conformations in understanding protein-ligand interactions. PubMed: 26150511DOI: 10.1073/pnas.1507317112 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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