6t36

Crystal structure of the PTPN3 PDZ domain bound to the HBV core protein C-terminal peptide

spinqualitylabelsall models 6t36, resolution 1.86Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6t36 is a 2 chain structure with sequence from Hepatitis B virus and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.86Å Ligands: BR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PTN3_HUMAN May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity. Publication Abstract from PubMed Interactions between the hepatitis B virus core protein (HBc) and host cell proteins are poorly understood, although they may be essential for the propagation of the virus and its pathogenicity. HBc has a C-terminal PDZ (PSD-95, Dlg1, ZO-1)-binding motif (PBM) that is responsible for interactions with host PDZ domain-containing proteins. In this work, we focused on the human protein tyrosine phosphatase non-receptor type 3 (PTPN3) and its interaction with HBc. We solved the crystal structure of the PDZ domain of PTPN3 in complex with the PBM of HBc, revealing a network of interactions specific to class I PDZ domains despite the presence of a C-terminal cysteine in this atypical PBM. We further showed that PTPN3 binds the HBc protein within capsids or as a homodimer. We demonstrate that overexpression of PTPN3 significantly affects HBV infection in HepG2 NTCP cells. Finally, we performed proteomics studies on both sides by pull-down assays and screening of a human PDZ domain library. We identified a pool of human PBM-containing proteins that might interact with PTPN3 in cells and that could be in competition with the HBc PBM during infection, and we also identified potential cellular partners of HBc through PDZ-PBM interactions. This study opens up many avenues of future investigations into the pathophysiology of HBV. Molecular basis of the interaction of the human tyrosine phosphatase PTPN3 with the hepatitis B virus core protein.,Genera M, Quioc-Salomon B, Nourisson A, Colcombet-Cazenave B, Haouz A, Mechaly A, Matondo M, Duchateau M, Konig A, Windisch MP, Neuveut C, Wolff N, Caillet-Saguy C Sci Rep. 2021 Jan 13;11(1):944. doi: 10.1038/s41598-020-79580-9. PMID:33441627 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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