2c36: Difference between revisions

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[[Image:2c36.png|left|200px]]


{{STRUCTURE_2c36| PDB=2c36 | SCENE= }}
==Structure of unliganded HSV gD reveals a mechanism for receptor- mediated activation of virus entry==
<StructureSection load='2c36' size='340' side='right'caption='[[2c36]], [[Resolution|resolution]] 2.11&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2c36]] is a 2 chain structure with sequence from [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=2C36 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C36 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]] 2.11&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2c36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c36 OCA], [https://pdbe.org/2c36 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c36 RCSB], [https://www.ebi.ac.uk/pdbsum/2c36 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c36 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GD_HHV1P GD_HHV1P] Envelope glycoprotein that binds to the potential host cell entry receptors TNFRSF14/HVEM, PVRL1 and 3-O-sulfated heparan sulfate. May trigger fusion with host membrane, by recruiting the fusion machinery composed of gB and gH/gL (By similarity).
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/c3/2c36_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2c36 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Herpes simplex virus (HSV) entry into cells requires binding of the envelope glycoprotein D (gD) to one of several cell surface receptors. The 50 C-terminal residues of the gD ectodomain are essential for virus entry, but not for receptor binding. We have determined the structure of an unliganded gD molecule that includes these C-terminal residues. The structure reveals that the C-terminus is anchored near the N-terminal region and masks receptor-binding sites. Locking the C-terminus in the position observed in the crystals by an intramolecular disulfide bond abolished receptor binding and virus entry, demonstrating that this region of gD moves upon receptor binding. Similarly, a point mutant that would destabilize the C-terminus structure was nonfunctional for entry, despite increased affinity for receptors. We propose that a controlled displacement of the gD C-terminus upon receptor binding is an essential feature of HSV entry, ensuring the timely activation of membrane fusion.


===STRUCTURE OF UNLIGANDED HSV GD REVEALS A MECHANISM FOR RECEPTOR-MEDIATED ACTIVATION OF VIRUS ENTRY===
Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry.,Krummenacher C, Supekar VM, Whitbeck JC, Lazear E, Connolly SA, Eisenberg RJ, Cohen GH, Wiley DC, Carfi A EMBO J. 2005 Dec 7;24(23):4144-53. Epub 2005 Nov 17. PMID:16292345<ref>PMID:16292345</ref>


{{ABSTRACT_PUBMED_16292345}}
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
==About this Structure==
<div class="pdbe-citations 2c36" style="background-color:#fffaf0;"></div>
[[2c36]] is a 2 chain structure of [[Glycoproteins B and D]] with sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C36 OCA].


==See Also==
==See Also==
*[[Glycoproteins B and D|Glycoproteins B and D]]
*[[Glycoproteins B and D|Glycoproteins B and D]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:016292345</ref><references group="xtra"/>
__TOC__
[[Category: Human herpesvirus 1]]
</StructureSection>
[[Category: Carfi, A.]]
[[Category: Human alphaherpesvirus 1]]
[[Category: Cohen, G H.]]
[[Category: Large Structures]]
[[Category: Connolly, S A.]]
[[Category: Carfi A]]
[[Category: Eisenberg, R J.]]
[[Category: Cohen GH]]
[[Category: Krummenacher, C.]]
[[Category: Connolly SA]]
[[Category: Lazear, E.]]
[[Category: Eisenberg RJ]]
[[Category: Supekar, V M.]]
[[Category: Krummenacher C]]
[[Category: Whitbeck, J C.]]
[[Category: Lazear E]]
[[Category: Wiley, D C.]]
[[Category: Supekar VM]]
[[Category: Glycoprotein]]
[[Category: Whitbeck JC]]
[[Category: Herpes]]
[[Category: Wiley DC]]
[[Category: Immunoglobulin-like]]
[[Category: Transmembrane]]
[[Category: Viral protein]]
[[Category: Virus]]

Latest revision as of 00:49, 21 November 2024

Structure of unliganded HSV gD reveals a mechanism for receptor- mediated activation of virus entry

2c36, resolution 2.11Å

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