Stimulator of interferon genes protein

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Revision as of 11:14, 29 January 2021

Human stimulator of interferon genes protein C-di-GMP-binding domain complex with GMP-AMP (PDB code 4loh)

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Updated on 29-January-2021

↑ Shang G, Zhang C, Chen ZJ, Bai XC, Zhang X. Cryo-EM structures of STING reveal its mechanism of activation by cyclic GMP-AMP. Nature. 2019 Mar 6. pii: 10.1038/s41586-019-0998-5. doi:, 10.1038/s41586-019-0998-5. PMID:30842659 doi:http://dx.doi.org/10.1038/s41586-019-0998-5
↑ Zhao B, Du F, Xu P, Shu C, Sankaran B, Bell SL, Liu M, Lei Y, Gao X, Fu X, Zhu F, Liu Y, Laganowsky A, Zheng X, Ji JY, West AP, Watson RO, Li P. A conserved PLPLRT/SD motif of STING mediates the recruitment and activation of TBK1. Nature. 2019 May;569(7758):718-722. doi: 10.1038/s41586-019-1228-x. Epub 2019 May, 22. PMID:31118511 doi:http://dx.doi.org/10.1038/s41586-019-1228-x
↑ Dobbs N, Burnaevskiy N, Chen D, Gonugunta VK, Alto NM, Yan N. STING Activation by Translocation from the ER Is Associated with Infection and Autoinflammatory Disease. Cell Host Microbe. 2015 Aug 12;18(2):157-68. doi: 10.1016/j.chom.2015.07.001., Epub 2015 Jul 30. PMID:26235147 doi:http://dx.doi.org/10.1016/j.chom.2015.07.001
↑ Kroeck KG, Sacco MD, Smith EW, Zhang X, Shoun D, Akhtar A, Darch SE, Cohen F, Andrews LD, Knox JE, Chen Y. Discovery of dual-activity small-molecule ligands of Pseudomonas aeruginosa LpxA and LpxD using SPR and X-ray crystallography. Sci Rep. 2019 Oct 29;9(1):15450. doi: 10.1038/s41598-019-51844-z. PMID:31664082 doi:http://dx.doi.org/10.1038/s41598-019-51844-z

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 == Structural highlights ==
-The biological assembly of UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase is <scene name='87/873780/Cv/4'>homotrimer</scene> (PDB code [[6uec]]). The 3D structure of LpxD complex with a ligand shows the binding site to be situated at <scene name='87/873780/Cv/6'>the interface of the crystallographic dimer</scene>. There are extensive polar interactions with LpxD as well as hydrogen bonds<ref>PMID:31664082</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 U-shaped cleft between the 2 subunits makes numerous interactions with the U-shaped ligand.  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:31664082</ref>.
 </StructureSection>