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| | <StructureSection load='5t1d' size='340' side='right'caption='[[5t1d]], [[Resolution|resolution]] 3.10Å' scene=''> | | <StructureSection load='5t1d' size='340' side='right'caption='[[5t1d]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5t1d]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Ebvb9 Ebvb9], [http://en.wikipedia.org/wiki/Ebvg Ebvg] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T1D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5T1D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5t1d]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_4 Human gammaherpesvirus 4], [https://en.wikipedia.org/wiki/Human_herpesvirus_4_strain_B95-8 Human herpesvirus 4 strain B95-8] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5T1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5T1D FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3phf|3phf]], [[3fd4|3fd4]], [[1kg0|1kg0]]</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gH, BXLF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10377 EBVB9]), gL, BKRF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10377 EBVB9]), BZLF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10376 EBVG])</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=5t1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t1d OCA], [https://pdbe.org/5t1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5t1d RCSB], [https://www.ebi.ac.uk/pdbsum/5t1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5t1d ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5t1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5t1d OCA], [http://pdbe.org/5t1d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5t1d RCSB], [http://www.ebi.ac.uk/pdbsum/5t1d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5t1d ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GH_EBVB9 GH_EBVB9]] The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. Fusion of EBV with B-lymphocytes requires the additional receptor-binding protein gp42, which forms a complex with gH/gL. May also be required for virus attachment to epithelial cells.<ref>PMID:11021994</ref> [[http://www.uniprot.org/uniprot/GP42_EBVG GP42_EBVG]] Plays a role in virion attachment to host B-lymphocytes, through binding to leukocyte antigen (HLA) class II and subsequently participates in fusion of the virion with host membranes. May act as a tropism switch that directs fusion with B-lymphocytes and inhibits fusion with epithelial cells (By similarity). [[http://www.uniprot.org/uniprot/GL_EBVB9 GL_EBVB9]] The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. Fusion of EBV with B-lymphocytes requires the additional receptor-binding protein gp42, which forms a complex with gH/gL. May also be required for virus attachment to epithelial cells (By similarity). | + | [https://www.uniprot.org/uniprot/GH_EBVB9 GH_EBVB9] The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. Fusion of EBV with B-lymphocytes requires the additional receptor-binding protein gp42, which forms a complex with gH/gL. May also be required for virus attachment to epithelial cells.<ref>PMID:11021994</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | Herpesvirus entry into host cells is mediated by multiple virally encoded receptor binding and membrane fusion glycoproteins. Despite their importance in host cell tropism and associated disease pathology, the underlying and essential interactions between these viral glycoproteins remain poorly understood. For Epstein-Barr virus (EBV), gHgL/gp42 complexes bind HLA class II to activate membrane fusion with B cells, but gp42 inhibits fusion and entry into epithelial cells. To clarify the mechanism by which gp42 controls the cell specificity of EBV infection, here we determined the structure of gHgL/gp42 complex bound to an anti-gHgL antibody (E1D1). The critical regulator of EBV tropism is the gp42 N-terminal domain, which tethers the HLA-binding domain to gHgL by wrapping around the exterior of three gH domains. Both the gp42 N-terminal domain and E1D1 selectively inhibit epithelial-cell fusion; however, they engage distinct surfaces of gHgL. These observations clarify key determinants of EBV host cell tropism.
| + | |
| - | | + | |
| - | Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.,Sathiyamoorthy K, Hu YX, Mohl BS, Chen J, Longnecker R, Jardetzky TS Nat Commun. 2016 Dec 8;7:13557. doi: 10.1038/ncomms13557. PMID:27929061<ref>PMID:27929061</ref>
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| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 5t1d" style="background-color:#fffaf0;"></div>
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| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ebvb9]] | + | [[Category: Human gammaherpesvirus 4]] |
| - | [[Category: Ebvg]] | + | [[Category: Human herpesvirus 4 strain B95-8]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
| - | [[Category: Jardetzky, T S]] | + | [[Category: Jardetzky TS]] |
| - | [[Category: Sathiyamoorthy, K]] | + | [[Category: Sathiyamoorthy K]] |
| - | [[Category: Epstein-barr virus]]
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| - | [[Category: Herpesvirus entry]]
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| - | [[Category: Membrane fusion]]
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| - | [[Category: Receptor binding]]
| + | |
| - | [[Category: Viral protein]]
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