2c3a: Difference between revisions
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New page: left|200px<br /> <applet load="2c3a" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c3a, resolution 2.50Å" /> '''STRUCTURE OF UNLIGA... |
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== | ==Structure of unliganded HSV gD reveals a mechanism for receptor- mediated activation of virus entry== | ||
Herpes simplex virus (HSV) entry into cells requires binding of the | <StructureSection load='2c3a' size='340' side='right'caption='[[2c3a]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2c3a]] 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=2C3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C3A 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]] 2.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=2c3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c3a OCA], [https://pdbe.org/2c3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c3a RCSB], [https://www.ebi.ac.uk/pdbsum/2c3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c3a 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/c3/2c3a_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=2c3a 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.,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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2c3a" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Glycoproteins B and D|Glycoproteins B and D]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Human alphaherpesvirus 1]] | |||
[[Category: Large Structures]] | |||
[[Category: Carfi A]] | |||
[[Category: Cohen GH]] | |||
[[Category: Connolly SA]] | |||
[[Category: Eisenberg RJ]] | |||
[[Category: Krummenacher C]] | |||
[[Category: Lazear E]] | |||
[[Category: Supekar VM]] | |||
[[Category: Whitbeck JC]] | |||
[[Category: Wiley DC]] | |||
Latest revision as of 10:48, 23 October 2024
Structure of unliganded HSV gD reveals a mechanism for receptor- mediated activation of virus entryStructure of unliganded HSV gD reveals a mechanism for receptor- mediated activation of virus entry
Structural highlights
FunctionGD_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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedHerpes 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.,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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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