View source for 3sku


==Herpes simplex virus glycoprotein D bound to the human receptor nectin-1==
<StructureSection load='3sku' size='340' side='right'caption='[[3sku]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sku]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1 Human alphaherpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SKU 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]] 4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <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=3sku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sku OCA], [https://pdbe.org/3sku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sku RCSB], [https://www.ebi.ac.uk/pdbsum/3sku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sku ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q991M3_HHV1 Q991M3_HHV1] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Binding of herpes simplex virus (HSV) glycoprotein D (gD) to a cell surface receptor is required to trigger membrane fusion during entry into host cells. Nectin-1 is a cell adhesion molecule and the main HSV receptor in neurons and epithelial cells. We report the structure of gD bound to nectin-1 determined by x-ray crystallography to 4.0 A resolution. The structure reveals that the nectin-1 binding site on gD differs from the binding site of the HVEM receptor. A surface on the first Ig-domain of nectin-1, which mediates homophilic interactions of Ig-like cell adhesion molecules, buries an area composed by residues from both the gD N- and C-terminal extensions. Phenylalanine 129, at the tip of the loop connecting beta-strands F and G of nectin-1, protrudes into a groove on gD, which is otherwise occupied by C-terminal residues in the unliganded gD and by N-terminal residues in the gD/HVEM complex. Notably, mutation of Phe129 to alanine prevents nectin-1 binding to gD and HSV entry. Together these data are consistent with previous studies showing that gD disrupts the normal nectin-1 homophilic interactions. Furthermore, the structure of the complex supports a model in which gD-receptor binding triggers HSV entry through receptor-mediated displacement of the gD C-terminal region.

Structure of herpes simplex virus glycoprotein d bound to the human receptor nectin-1.,Di Giovine P, Settembre EC, Bhargava AK, Luftig MA, Lou H, Cohen GH, Eisenberg RJ, Krummenacher C, Carfi A PLoS Pathog. 2011 Sep;7(9):e1002277. Epub 2011 Sep 29. PMID:21980294<ref>PMID:21980294</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3sku" style="background-color:#fffaf0;"></div>

==See Also==
*[[Glycoproteins B and D|Glycoproteins B and D]]
*[[Poliovirus receptor-related protein|Poliovirus receptor-related protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human alphaherpesvirus 1]]
[[Category: Large Structures]]
[[Category: Bhargava AK]]
[[Category: Carfi A]]
[[Category: Cohen GH]]
[[Category: Di Giovine P]]
[[Category: Eisenberg RJ]]
[[Category: Krummenacher C]]
[[Category: Lou H]]
[[Category: Luftig MA]]
[[Category: Settembre EC]]