4F5Y
Crystal structure of human STING CTD complex with C-di-GMP
Summary for 4F5Y
Entry DOI | 10.2210/pdb4f5y/pdb |
Related | 4F5W |
Descriptor | Transmembrane protein 173, CALCIUM ION, 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), ... (4 entities in total) |
Functional Keywords | innate immunity, sting, c-di-gmp, immune system |
Biological source | Homo sapiens (human) |
Cellular location | Endoplasmic reticulum membrane; Multi-pass membrane protein: Q86WV6 |
Total number of polymer chains | 2 |
Total formula weight | 55249.80 |
Authors | |
Primary citation | Shang, G.,Zhu, D.,Li, N.,Zhang, J.,Zhu, C.,Lu, D.,Liu, C.,Yu, Q.,Zhao, Y.,Xu, S.,Gu, L. Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP Nat.Struct.Mol.Biol., 19:725-727, 2012 Cited by PubMed Abstract: STING functions as both an adaptor protein signaling cytoplasmic double-stranded DNA and a direct immunosensor of cyclic diguanylate monophosphate (c-di-GMP). The crystal structures of the C-terminal domain of human STING (STING(CTD)) and its complex with c-di-GMP reveal how STING recognizes c-di-GMP. In response to c-di-GMP binding, two surface loops, which serve as a gate and latch of the cleft formed by the dimeric STING(CTD), undergo rearrangements to interact with the ligand. PubMed: 22728660DOI: 10.1038/nsmb.2332 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.396 Å) |
Structure validation
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