3m1c
From Proteopedia
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- | {{STRUCTURE_3m1c| PDB=3m1c | SCENE= }} | ||
- | ===Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL=== | ||
- | {{ABSTRACT_PUBMED_20601960}} | ||
- | == | + | ==Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL== |
- | [[http://www.uniprot.org/uniprot/GH_HHV2H GH_HHV2H | + | <StructureSection load='3m1c' size='340' side='right'caption='[[3m1c]], [[Resolution|resolution]] 3.00Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3m1c]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_herpesvirus_2_strain_HG52 Human herpesvirus 2 strain HG52]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3M1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M1C 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]] 3Å</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>, <scene name='pdbligand=XYL:D-XYLITOL'>XYL</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=3m1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m1c OCA], [https://pdbe.org/3m1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m1c RCSB], [https://www.ebi.ac.uk/pdbsum/3m1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m1c ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/GH_HHV2H GH_HHV2H] 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 of gD to one of its receptors, membrane fusion is mediated by the fusion machinery composed at least 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 (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/m1/3m1c_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=3m1c ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Herpesviruses, which cause many incurable diseases, infect cells by fusing viral and cellular membranes. Whereas most other enveloped viruses use a single viral catalyst called a fusogen, herpesviruses, inexplicably, require two conserved fusion-machinery components, gB and the heterodimer gH-gL, plus other nonconserved components. gB is a class III viral fusogen, but unlike other members of its class, it does not function alone. We determined the crystal structure of the gH ectodomain bound to gL from herpes simplex virus 2. gH-gL is an unusually tight complex with a unique architecture that, unexpectedly, does not resemble any known viral fusogen. Instead, we propose that gH-gL activates gB for fusion, possibly through direct binding. Formation of a gB-gH-gL complex is critical for fusion and is inhibited by a neutralizing antibody, making the gB-gH-gL interface a promising antiviral target. | ||
- | + | Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL.,Chowdary TK, Cairns TM, Atanasiu D, Cohen GH, Eisenberg RJ, Heldwein EE Nat Struct Mol Biol. 2010 Jul;17(7):882-8. Epub 2010 Jul 4. PMID:20601960<ref>PMID:20601960</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | < | + | </div> |
- | [[Category: Human herpesvirus 2]] | + | <div class="pdbe-citations 3m1c" style="background-color:#fffaf0;"></div> |
- | [[Category: | + | == References == |
- | [[Category: | + | <references/> |
- | [[Category: | + | __TOC__ |
- | + | </StructureSection> | |
- | + | [[Category: Human herpesvirus 2 strain HG52]] | |
- | + | [[Category: Large Structures]] | |
- | + | [[Category: Chowdary TK]] | |
- | + | [[Category: Heldwein EE]] | |
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Current revision
Crystal structure of the conserved herpesvirus fusion regulator complex gH-gL
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