5t1d

From Proteopedia

(Difference between revisions)

Revision as of 09:21, 4 December 2019

Crystal structure of EBV gHgL/gp42/E1D1 complex

Structural highlights

5t1d is a 5 chain structure with sequence from Ebvb9, Ebvg and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3phf, 3fd4, 1kg0
Gene:	gH, BXLF2 (EBVB9), gL, BKRF2 (EBVB9), BZLF2 (EBVG)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] [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). [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

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^[2]

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

References

↑ Oda T, Imai S, Chiba S, Takada K. Epstein-Barr virus lacking glycoprotein gp85 cannot infect B cells and epithelial cells. Virology. 2000 Oct 10;276(1):52-8. PMID:11021994 doi:http://dx.doi.org/10.1006/viro.2000.0531
↑ Sathiyamoorthy K, Hu YX, Mohl BS, Chen J, Longnecker R, Jardetzky TS. Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins. Nat Commun. 2016 Dec 8;7:13557. doi: 10.1038/ncomms13557. PMID:27929061 doi:http://dx.doi.org/10.1038/ncomms13557

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5t1d"

@@ Line 1: / Line 1: @@
 ==Crystal structure of EBV gHgL/gp42/E1D1 complex==
-<StructureSection load='5t1d' size='340' side='right' caption='[[5t1d]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
+<StructureSection load='5t1d' size='340' side='right'caption='[[5t1d]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
 == 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>
@@ Line 26: / Line 26: @@
 [[Category: Ebvb9]]
 [[Category: Ebvg]]
+[[Category: Large Structures]]
 [[Category: Mus musculus]]
 [[Category: Jardetzky, T S]]

5t1d

From Proteopedia

Revision as of 09:21, 4 December 2019

Crystal structure of EBV gHgL/gp42/E1D1 complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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