View source for 2lqy


==Structure and orientation of the gH625-644 membrane interacting region of herpes simplex virus type 1 in a membrane mimetic system.==
<StructureSection load='2lqy' size='340' side='right'caption='[[2lqy]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2lqy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1 Human alphaherpesvirus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2LQY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2lqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2lqy OCA], [https://pdbe.org/2lqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2lqy RCSB], [https://www.ebi.ac.uk/pdbsum/2lqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2lqy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GH_HHV11 GH_HHV11] The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis.[HAMAP-Rule:MF_04033]<ref>PMID:17548810</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Glycoprotein H (gH) of the herpes simplex virus type 1 is involved in the complex mechanism of membrane fusion of the viral envelope with host cells. The virus requires four glycoproteins (gB, gD, gH, gL) to execute fusion and the role played by gH remains mysterious. Mutational studies have revealed several regions of gH ectodomain required for fusion and identified the segment from amino acid 625 to 644 as the most fusogenic region. Here, we studied the behavior in a membrane-mimicking DPC micellar environment of a peptide encompassing this region (gH625-644) and determined its NMR solution structure and its orientation within the micelles.

Structure and Orientation of the gH625-644 Membrane Interacting Region of Herpes Simplex Virus Type 1 in a Membrane Mimetic System.,Galdiero S, Russo L, Falanga A, Cantisani M, Vitiello M, Fattorusso R, Malgieri G, Galdiero M, Isernia C Biochemistry. 2012 Apr 10;51(14):3121-8. Epub 2012 Mar 23. PMID:22397737<ref>PMID:22397737</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2lqy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human alphaherpesvirus 1]]
[[Category: Large Structures]]
[[Category: Cantisani M]]
[[Category: Falanga A]]
[[Category: Fattorusso R]]
[[Category: Galdiero M]]
[[Category: Galdiero S]]
[[Category: Isernia C]]
[[Category: Malgieri G]]
[[Category: Russo L]]
[[Category: Vitiello M]]