6t36: Difference between revisions
New page: '''Unreleased structure''' The entry 6t36 is ON HOLD Authors: Description: Category: Unreleased Structures |
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==Crystal structure of the PTPN3 PDZ domain bound to the HBV core protein C-terminal peptide== | |||
<StructureSection load='6t36' size='340' side='right'caption='[[6t36]], [[Resolution|resolution]] 1.86Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6t36]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_B_virus Hepatitis B virus] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T36 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.86Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BR:BROMIDE+ION'>BR</scene></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6t36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t36 OCA], [https://pdbe.org/6t36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t36 RCSB], [https://www.ebi.ac.uk/pdbsum/6t36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t36 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PTN3_HUMAN PTN3_HUMAN] May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity. | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:33441627</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6t36" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Hepatitis B virus]] | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Caillet-Saguy C]] | |||
[[Category: Genera M]] | |||
[[Category: Haouz A]] | |||
[[Category: Mechaly A]] | |||
Latest revision as of 15:53, 24 January 2024
Crystal structure of the PTPN3 PDZ domain bound to the HBV core protein C-terminal peptideCrystal structure of the PTPN3 PDZ domain bound to the HBV core protein C-terminal peptide
Structural highlights
FunctionPTN3_HUMAN May act at junctions between the membrane and the cytoskeleton. Possesses tyrosine phosphatase activity. Publication Abstract from PubMedInteractions 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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