2hg0: Difference between revisions

<StructureSection load='2hg0' size='340' side='right'caption='[[2hg0]], [[Resolution|resolution]] 3.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[2hg0]] 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=2HG0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HG0 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&#8491;</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>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</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=2hg0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hg0 OCA], [https://pdbe.org/2hg0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hg0 RCSB], [https://www.ebi.ac.uk/pdbsum/2hg0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hg0 ProSAT]</span></td></tr>

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The envelope glycoprotein (E) of West Nile virus (WNV) undergoes a conformational rearrangement triggered by low pH that results in a class II fusion event required for viral entry. Herein we present the 3.0-A crystal structure of the ectodomain of WNV E, which reveals insights into the flavivirus life cycle. We found that WNV E adopts a three-domain architecture that is shared by the E proteins from dengue and tick-borne encephalitis viruses and forms a rod-shaped configuration similar to that observed in immature flavivirus particles. Interestingly, the single N-linked glycosylation site on WNV E is displaced by a novel alpha-helix, which could potentially alter lectin-mediated attachment. The localization of histidines within the hinge regions of E implicates these residues in pH-induced conformational transitions. Most strikingly, the WNV E ectodomain crystallized as a monomer, in contrast to other flavivirus E proteins, which have crystallized as antiparallel dimers. WNV E assembles in a crystalline lattice of perpendicular molecules, with the fusion loop of one E protein buried in a hydrophobic pocket at the DI-DIII interface of another. Dimeric E proteins pack their fusion loops into analogous pockets at the dimer interface. We speculate that E proteins could pivot around the fusion loop-pocket junction, allowing virion conformational transitions while minimizing fusion loop exposure.

Crystal structure of the West Nile virus envelope glycoprotein.,Nybakken GE, Nelson CA, Chen BR, Diamond MS, Fremont DH J Virol. 2006 Dec;80(23):11467-74. Epub 2006 Sep 20. PMID:16987985<ref>PMID:16987985</ref>

==See Also==

*[[Lysozyme 3D structures|Lysozyme 3D structures]]

== References ==

<references/>

</StructureSection>

[[Category: Large Structures]]

[[Category: West Nile virus]]

[[Category: Chen BR]]

[[Category: Diamond MS]]

[[Category: Fremont DH]]

[[Category: Nelson CA]]

[[Category: Nybakken GE]]