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| | <StructureSection load='3phf' size='340' side='right'caption='[[3phf]], [[Resolution|resolution]] 3.58Å' scene=''> | | <StructureSection load='3phf' size='340' side='right'caption='[[3phf]], [[Resolution|resolution]] 3.58Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3phf]] is a 32 chain structure with sequence from [https://en.wikipedia.org/wiki/Ebvg Ebvg]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PHF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3phf]] is a 32 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_gammaherpesvirus_4 Human gammaherpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3PHF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3PHF FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3m1c|3m1c]]</div></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]] 3.58Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BXLF2, gH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10376 EBVG]), BKRF2, GL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10376 EBVG])</td></tr>
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| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3phf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3phf OCA], [https://pdbe.org/3phf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3phf RCSB], [https://www.ebi.ac.uk/pdbsum/3phf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3phf ProSAT]</span></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=3phf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3phf OCA], [https://pdbe.org/3phf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3phf RCSB], [https://www.ebi.ac.uk/pdbsum/3phf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3phf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> [[https://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/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). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ebvg]] | + | [[Category: Human gammaherpesvirus 4]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jardetzky, T S]] | + | [[Category: Jardetzky TS]] |
| - | [[Category: Kirschner, A N]] | + | [[Category: Kirschner AN]] |
| - | [[Category: Matsuura, H]] | + | [[Category: Matsuura H]] |
| - | [[Category: Glycoprotein]]
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| - | [[Category: Membrane fusion]]
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| - | [[Category: Viral protein]]
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| - | [[Category: Virus entry]]
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| Structural highlights
Function
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).
Publication Abstract from PubMed
The Epstein-Barr virus (EBV) is a gamma-herpesvirus that infects B cells and epithelial cells and that has been linked to malignancies in both cell types in vivo. EBV, like other herpesviruses, has three glycoproteins, glycoprotein B (gB), gH, and gL, that form the core membrane fusion machinery mediating viral penetration into the cell. The gH and gL proteins associate to form a heterodimeric complex, which is necessary for efficient membrane fusion and also implicated in direct binding to epithelial cell receptors required for viral entry. To gain insight into the mechanistic role of gH/gL, we determined the crystal structure of the EBV gH/gL complex. The structure is comprised of four domains organized along the longest axis of the molecule. Comparisons with homologous HSV-2 gH/gL and partial pseudorabies virus gH structures support the domain boundaries determined for the EBV gH/gL structure and illustrate significant differences in interdomain packing angles. The gL subunit and N-terminal residues of gH form a globular domain at one end of the structure, implicated in interactions with gB and activation of membrane fusion. The C-terminal domain of gH, proximal to the viral membrane, is also implicated in membrane fusion. The gH/gL structure locates an integrin binding motif, implicated in epithelial cell entry, on a prominent loop in the central region of the structure. Multiple regions of gH/gL, including its two extreme ends, are functionally important, consistent with the multiple roles of gH/gL in EBV entry.
Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex.,Matsuura H, Kirschner AN, Longnecker R, Jardetzky TS Proc Natl Acad Sci U S A. 2010 Dec 28;107(52):22641-6. Epub 2010 Dec 13. PMID:21149717[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Matsuura H, Kirschner AN, Longnecker R, Jardetzky TS. Crystal structure of the Epstein-Barr virus (EBV) glycoprotein H/glycoprotein L (gH/gL) complex. Proc Natl Acad Sci U S A. 2010 Dec 28;107(52):22641-6. Epub 2010 Dec 13. PMID:21149717 doi:10.1073/pnas.1011806108
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