8cni

PHT1 in the outward facing conformation, bound to Sb27

spinqualitylabelsall models 8cni, resolution 3.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cni is a 3 chain structure with sequence from Escherichia coli and Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 3.35Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A8V0ZFZ8_CHICK Publication Abstract from PubMed PHT1 is a histidine /oligopeptide transporter with an essential role in Toll-like receptor innate immune responses. It can act as a receptor by recruiting the adaptor protein TASL which leads to type I interferon production via IRF5. Persistent stimulation of this signalling pathway is known to be involved in the pathogenesis of systemic lupus erythematosus (SLE). Understanding how PHT1 recruits TASL at the molecular level, is therefore clinically important for the development of therapeutics against SLE and other autoimmune diseases. Here we present the Cryo-EM structure of PHT1 stabilized in the outward-open conformation. By combining biochemical and structural modeling techniques we propose a model of the PHT1-TASL complex, in which the first 16 N-terminal TASL residues fold into a helical structure that bind in the central cavity of the inward-open conformation of PHT1. This work provides critical insights into the molecular basis of PHT1/TASL mediated type I interferon production. Molecular basis of TASL recruitment by the peptide/histidine transporter 1, PHT1.,Custodio TF, Killer M, Yu D, Puente V, Teufel DP, Pautsch A, Schnapp G, Grundl M, Kosinski J, Low C Nat Commun. 2023 Sep 14;14(1):5696. doi: 10.1038/s41467-023-41420-5. PMID:37709742 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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