2i69
From Proteopedia
(Difference between revisions)
| (9 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | [[Image:2i69.gif|left|200px]] | ||
| - | + | ==Crystal structure of the West Nile virus envelope glycoprotein== | |
| - | + | <StructureSection load='2i69' size='340' side='right'caption='[[2i69]], [[Resolution|resolution]] 3.11Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[2i69]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/West_Nile_virus West Nile virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2I69 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]] 3.11Å</td></tr> | |
| - | - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUL:BETA-L-FUCOSE'>FUL</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=2i69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i69 OCA], [https://pdbe.org/2i69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2i69 RCSB], [https://www.ebi.ac.uk/pdbsum/2i69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2i69 ProSAT]</span></td></tr> | |
| - | + | </table> | |
| - | ''' | + | == Function == |
| - | + | [https://www.uniprot.org/uniprot/Q80QJ9_WNV Q80QJ9_WNV] | |
| - | + | <div style="background-color:#fffaf0;"> | |
| - | == | + | == Publication Abstract from PubMed == |
West Nile virus, a member of the Flavivirus genus, causes fever that can progress to life-threatening encephalitis. The major envelope glycoprotein, E, of these viruses mediates viral attachment and entry by membrane fusion. We have determined the crystal structure of a soluble fragment of West Nile virus E. The structure adopts the same overall fold as that of the E proteins from dengue and tick-borne encephalitis viruses. The conformation of domain II is different from that in other prefusion E structures, however, and resembles the conformation of domain II in postfusion E structures. The epitopes of neutralizing West Nile virus-specific antibodies map to a region of domain III that is exposed on the viral surface and has been implicated in receptor binding. In contrast, we show that certain recombinant therapeutic antibodies, which cross-neutralize West Nile and dengue viruses, bind a peptide from domain I that is exposed only during the membrane fusion transition. By revealing the details of the molecular landscape of the West Nile virus surface, our structure will assist the design of antiviral vaccines and therapeutics. | West Nile virus, a member of the Flavivirus genus, causes fever that can progress to life-threatening encephalitis. The major envelope glycoprotein, E, of these viruses mediates viral attachment and entry by membrane fusion. We have determined the crystal structure of a soluble fragment of West Nile virus E. The structure adopts the same overall fold as that of the E proteins from dengue and tick-borne encephalitis viruses. The conformation of domain II is different from that in other prefusion E structures, however, and resembles the conformation of domain II in postfusion E structures. The epitopes of neutralizing West Nile virus-specific antibodies map to a region of domain III that is exposed on the viral surface and has been implicated in receptor binding. In contrast, we show that certain recombinant therapeutic antibodies, which cross-neutralize West Nile and dengue viruses, bind a peptide from domain I that is exposed only during the membrane fusion transition. By revealing the details of the molecular landscape of the West Nile virus surface, our structure will assist the design of antiviral vaccines and therapeutics. | ||
| - | + | Crystal structure of west nile virus envelope glycoprotein reveals viral surface epitopes.,Kanai R, Kar K, Anthony K, Gould LH, Ledizet M, Fikrig E, Marasco WA, Koski RA, Modis Y J Virol. 2006 Nov;80(22):11000-8. Epub 2006 Aug 30. PMID:16943291<ref>PMID:16943291</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2i69" style="background-color:#fffaf0;"></div> |
| - | [[Category: West | + | == References == |
| - | [[Category: Kanai | + | <references/> |
| - | [[Category: Modis | + | __TOC__ |
| - | + | </StructureSection> | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: West Nile virus]] | |
| - | + | [[Category: Kanai R]] | |
| - | + | [[Category: Modis Y]] | |
| - | + | ||
| - | + | ||
Current revision
Crystal structure of the West Nile virus envelope glycoprotein
| |||||||||||
