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7cze

From Proteopedia

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Current revision

Crystal structure of Epstein-Barr virus (EBV) gHgL and in complex with the ligand binding domian (LBD) of EphA2

Structural highlights

7cze is a 12 chain structure with sequence from Homo sapiens and Human herpesvirus 4 strain B95-8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 human gamma-herpesviruses Kaposi sarcoma associated herpesvirus (KSHV) and Epstein-Barr virus (EBV) are associated with many human malignancies. Viral glycoprotein H (gH) and glycoprotein L (gL) are crucial for the cell tropism by binding to specific receptors. Recently, EphA2 was identified as the specific entry receptor for both KSHV and EBV. Here, we characterized the crystal structures of KSHV gHgL or EBV gHgL in complex with the ligand binding domain (LBD) of EphA2. Both KSHV and EBV gHgL bind to the channel and peripheral regions of LBD primarily using gL. Extensive interactions with more contacts contribute to the higher affinity of KSHV gHgL to LBD than that of EBV gHgL. These binding characteristics were verified using cell-based fusion assays with mutations in key EphA2 residues. Our experiments suggest that multiple animal gamma-herpesviruses could use EphA2 as an entry receptor, implying a potential threat to human health.

Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses.,Su C, Wu L, Chai Y, Qi J, Tan S, Gao GF, Song H, Yan J Nat Commun. 2020 Nov 24;11(1):5964. doi: 10.1038/s41467-020-19617-9. PMID:33235207^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Su C, Wu L, Chai Y, Qi J, Tan S, Gao GF, Song H, Yan J. Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses. Nat Commun. 2020 Nov 24;11(1):5964. PMID:33235207 doi:10.1038/s41467-020-19617-9

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7cze"

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 == 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).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

7cze

From Proteopedia

Current revision

Crystal structure of Epstein-Barr virus (EBV) gHgL and in complex with the ligand binding domian (LBD) of EphA2

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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