View source for 4myv


==Free HSV-2 gD structure==
<StructureSection load='4myv' size='340' side='right'caption='[[4myv]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4myv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_2_strain_333 Human herpesvirus 2 strain 333]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MYV 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]] 1.801&#8491;</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4myv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4myv OCA], [https://pdbe.org/4myv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4myv RCSB], [https://www.ebi.ac.uk/pdbsum/4myv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4myv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GD_HHV23 GD_HHV23] Envelope glycoprotein that binds to the potential host cell entry receptors TNFRSF14/HVEM, PVRL1 and PVRL1. May trigger fusion with host membrane, by recruiting the fusion machinery composed of gB and gH/gL (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Herpes simplex virus type 1 (HSV-1) and type 2 (HSV-2) are among the most prevalent human pathogens. Both viruses can recognize, via the surface envelope glycoprotein D (gD), human nectin-1 as a functional receptor. Previous studies have successfully elucidated the molecular basis of the binding between HSV-1 gD and nectin-1 by co-crystallography. Despite a high sequence identity between HSV-1 and -2 gDs, the atomic inter-molecule details for HSV-2-gD/nectin-1 interaction remain elusive. Here, we reported the crystal structures of both the unbound and the nectin-1-bound HSV-2 gD. The free gD structure expectedly comprises an IgV-like core and the surface-exposed terminal extensions as observed in its HSV-1 counterpart, but lacks traceable electron densities for a large portion of the terminal elements. These terminal residues were clearly traced in the complex structure as a definitive loop in the N-terminus and an alpha-helix in the C-terminus, thereby showing a conserved nectin-1-binding mode as reported for HSV-1 gD. The interface residues in nectin-1 were further mutated and tested for the gD-interaction by surface plasmon resonance. The resultant binding patterns were similar between HSV-1 and -2 gDs, further supporting a homologous receptor-binding basis by the two viruses for nectin-1. These data, together with a cell-based fusion assay showing a cross-inhibition of the gD/nectin-1 mediated cell-cell fusion by soluble HSV-1 and -2 gDs, provided solid structural and functional evidence that HSV-1/-2 recognizes nectin-1 via the same binding mode. Finally, we also demonstrated that nectin-1 I80 is an important residue involved in gD interaction. IMPORTANCE: Despite intensified studies, a detailed picture of the molecular features in the HSV-2-gD/nectin-1 interaction remains unavailable. Previous work focused on HSV-1 gD, which folds into an IgV-like core with large terminal extensions and utilizes the extension elements to engage nectin-1. Here, we reported the crystal structures of HSV-2 gD in both the free and the nectin-1-bound forms. The atomic inter-molecule details for HSV-2-gD/nectin-1 interaction were clearly presented. The observed binding mode is identical to that reported for its HSV-1 counterpart. This structural observation was further supported by our comparative functional assays showing that nectin-1 mutations similarly affect the ligand/receptor interaction of both virus gDs. Taken together, we provided comprehensive structural and functional data demonstrating a conserved receptor-binding mode between HSV-1 and -2 for nectin-1. Our results also indicate that the tropism-difference between the two viruses likely arises from other aspects rather than the gD/nectin-1 binding-features.

Crystal structure of HSV-2 gD bound to nectin-1 reveals a conserved mode of receptor recognition.,Lu G, Zhang N, Qi J, Li Y, Chen Z, Zheng C, Gao GF, Yan J J Virol. 2014 Sep 17. pii: JVI.01906-14. PMID:25231300<ref>PMID:25231300</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4myv" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glycoproteins B and D|Glycoproteins B and D]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human herpesvirus 2 strain 333]]
[[Category: Large Structures]]
[[Category: Chen Z]]
[[Category: Gao GF]]
[[Category: Li Y]]
[[Category: Lu G]]
[[Category: Qi J]]
[[Category: Yan J]]
[[Category: Zhang N]]
[[Category: Zheng C]]