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| | ==Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation== | | ==Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation== |
| - | <StructureSection load='3g7t' size='340' side='right' caption='[[3g7t]], [[Resolution|resolution]] 3.50Å' scene=''> | + | <StructureSection load='3g7t' size='340' side='right'caption='[[3g7t]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3g7t]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_1 Dengue virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G7T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3G7T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3g7t]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_1 Dengue virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3G7T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3G7T FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.5Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">E ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11053 Dengue virus 1])</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></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3g7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g7t OCA], [http://pdbe.org/3g7t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3g7t RCSB], [http://www.ebi.ac.uk/pdbsum/3g7t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3g7t ProSAT]</span></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=3g7t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3g7t OCA], [https://pdbe.org/3g7t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3g7t RCSB], [https://www.ebi.ac.uk/pdbsum/3g7t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3g7t ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/Q5USP2_9FLAV Q5USP2_9FLAV]] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS013754_004_099774] | + | [https://www.uniprot.org/uniprot/Q689G3_9FLAV Q689G3_9FLAV] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS013754_004_099774] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Dengue virus 1]] | | [[Category: Dengue virus 1]] |
| - | [[Category: Modis, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Beta sandwich]] | + | [[Category: Modis Y]] |
| - | [[Category: Envelope protein]]
| + | |
| - | [[Category: Fusion loop]]
| + | |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Igc domain]]
| + | |
| - | [[Category: Membrane]]
| + | |
| - | [[Category: Membrane anchor]]
| + | |
| - | [[Category: Membrane fusion protein]]
| + | |
| - | [[Category: Transmembrane]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Virion]]
| + | |
| Structural highlights
Function
Q689G3_9FLAV Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS013754_004_099774]
Publication Abstract from PubMed
Dengue virus relies on a conformational change in its envelope protein, E, to fuse the viral lipid membrane with the endosomal membrane and thereby deliver the viral genome into the cytosol. We have determined the crystal structure of a soluble fragment E (sE) of dengue virus type 1 (DEN-1). The protein is in the postfusion conformation even though it was not exposed to a lipid membrane or detergent. At the domain I-domain III interface, 4 polar residues form a tight cluster that is absent in other flaviviral postfusion structures. Two of these residues, His-282 and His-317, are conserved in flaviviruses and are part of the "pH sensor" that triggers the fusogenic conformational change in E, at the reduced pH of the endosome. In the fusion loop, Phe-108 adopts a distinct conformation, forming additional trimer contacts and filling the bowl-shaped concavity observed at the tip of the DEN-2 sE trimer.
Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion.,Nayak V, Dessau M, Kucera K, Anthony K, Ledizet M, Modis Y J Virol. 2009 May;83(9):4338-44. Epub 2009 Feb 25. PMID:19244332[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Nayak V, Dessau M, Kucera K, Anthony K, Ledizet M, Modis Y. Crystal structure of dengue virus type 1 envelope protein in the postfusion conformation and its implications for membrane fusion. J Virol. 2009 May;83(9):4338-44. Epub 2009 Feb 25. PMID:19244332 doi:10.1128/JVI.02574-08
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