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| | ==NMR Structure of Domain III of the West Nile Virus Envelope Protein, Strain 385-99== | | ==NMR Structure of Domain III of the West Nile Virus Envelope Protein, Strain 385-99== |
| - | <StructureSection load='1s6n' size='340' side='right'caption='[[1s6n]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='1s6n' size='340' side='right'caption='[[1s6n]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1s6n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/West_nile_virus_strain_385-99 West nile virus strain 385-99]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1S6N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1s6n]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/West_Nile_virus_strain_385-99 West Nile virus strain 385-99]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1S6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S6N FirstGlance]. <br> |
| - | </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=1s6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s6n OCA], [http://pdbe.org/1s6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1s6n RCSB], [http://www.ebi.ac.uk/pdbsum/1s6n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1s6n ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1s6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s6n OCA], [https://pdbe.org/1s6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s6n RCSB], [https://www.ebi.ac.uk/pdbsum/1s6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s6n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q913C7_WNV Q913C7_WNV] |
| | <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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: West nile virus strain 385-99]] | + | [[Category: West Nile virus strain 385-99]] |
| - | [[Category: Barrett, A D]] | + | [[Category: Barrett AD]] |
| - | [[Category: Beasley, D W]] | + | [[Category: Beasley DW]] |
| - | [[Category: Gorenstein, D G]] | + | [[Category: Gorenstein DG]] |
| - | [[Category: Holbrook, M R]] | + | [[Category: Holbrook MR]] |
| - | [[Category: Kallick, D A]] | + | [[Category: Kallick DA]] |
| - | [[Category: Volk, D E]] | + | [[Category: Volk DE]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Flavivirus]]
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| - | [[Category: Viral protein]]
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| Structural highlights
Function
Q913C7_WNV
Publication Abstract from PubMed
The solution structure of domain III from the New York West Nile virus strain 385-99 (WN-rED3) has been determined by NMR methods. The West Nile domain III structure is a beta-barrel structure formed from seven anti-parallel beta-strands in two beta-sheets. One anti-parallel beta-sheet consists of beta-strands beta1 (Phe(299)-Asp(307)), beta2 (Val(313)-Tyr(319)), beta4 (Arg(354)-Leu(355)), and beta5 (Lys(370)-Glu(376)) arranged so that beta2 is flanked on either side by beta1 and beta5. The short beta4 flanks the end of the remaining side of beta5. The remaining anti-parallel beta-sheet is formed from strands beta3 (Ile(340)-Val(343)), beta6 (Gly(380)-Arg(388)), and beta7 (Gln(391)-Lys(399)) arranged with beta6 at the center. Residues implicated in antigenic differences between different West Nile virus strains (and other flaviviruses) and neutralization are located on the outer surface of the protein. Characterization of the binding of monoclonal antibodies to WN-rED3 mutants, which were identified through neutralization escape experiments, indicate that antibody neutralization directly correlates with binding affinities. These studies provide an insight into theoretical virus-receptor interaction points, structure of immunogenic determinants, and potential targets for antiviral agents against West Nile virus and highlight differences between West Nile virus and other flavivirus structures that may represent critical determinants of virulence.
Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus.,Volk DE, Beasley DW, Kallick DA, Holbrook MR, Barrett AD, Gorenstein DG J Biol Chem. 2004 Sep 10;279(37):38755-61. Epub 2004 Jun 9. PMID:15190071[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Volk DE, Beasley DW, Kallick DA, Holbrook MR, Barrett AD, Gorenstein DG. Solution structure and antibody binding studies of the envelope protein domain III from the New York strain of West Nile virus. J Biol Chem. 2004 Sep 10;279(37):38755-61. Epub 2004 Jun 9. PMID:15190071 doi:http://dx.doi.org/10.1074/jbc.M402385200
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