4f5w | pdb_00004f5w

Crystal structure of ligand free human STING CTD

spinqualitylabelsall models 4f5w, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4f5w is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Related: 4f5y Gene: TMEM173, ERIS, MITA, STING (Homo sapiens) Resources: FirstGlance, OCA, RCSB, PDBsum Function [STING_HUMAN] Facilitator of innate immune signaling that acts as a sensor of cytosolic DNA from bacteria and viruses and promotes the production of type I interferon (IFN-alpha and IFN-beta). Innate immune response is triggered in response to non-CpG double-stranded DNA from viruses and bacteria delivered to the cytoplasm. Acts by recognizing and binding cyclic di-GMP (c-di-GMP), a second messenger produced by bacteria, and cyclic GMP-AMP (cGAMP), a messenger produced in response to DNA virus in the cytosol: upon binding of c-di-GMP or cGAMP, autoinhibition is alleviated and TMEM173/STING is able to activate both NF-kappa-B and IRF3 transcription pathways to induce expression of type I interferon and exert a potent anti-viral state. May be involved in translocon function, the translocon possibly being able to influence the induction of type I interferons. May be involved in transduction of apoptotic signals via its association with the major histocompatibility complex class II (MHC-II). Mediates death signaling via activation of the extracellular signal-regulated kinase (ERK) pathway. Publication Abstract from PubMed 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. Crystal structures of STING protein reveal basis for recognition of cyclic di-GMP.,Shang G, Zhu D, Li N, Zhang J, Zhu C, Lu D, Liu C, Yu Q, Zhao Y, Xu S, Gu L Nat Struct Mol Biol. 2012 Jun 24;19(7):725-7. doi: 10.1038/nsmb.2332. PMID:22728660 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Stimulator of interferon genes

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