1ztx

From Proteopedia

(Difference between revisions)

Current revision

West Nile Virus Envelope Protein DIII in complex with neutralizing E16 antibody Fab

Structural highlights

1ztx is a 3 chain structure with sequence from Mus musculus and West Nile virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q91KZ4_WNV

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

West Nile virus is a mosquito-borne flavivirus closely related to the human epidemic-causing dengue, yellow fever and Japanese encephalitis viruses. In establishing infection these icosahedral viruses undergo endosomal membrane fusion catalysed by envelope glycoprotein rearrangement of the putative receptor-binding domain III (DIII) and exposure of the hydrophobic fusion loop. Humoral immunity has an essential protective function early in the course of West Nile virus infection. Here, we investigate the mechanism of neutralization by the E16 monoclonal antibody that specifically binds DIII. Structurally, the E16 antibody Fab fragment engages 16 residues positioned on four loops of DIII, a consensus neutralizing epitope sequence conserved in West Nile virus and distinct in other flaviviruses. The E16 epitope protrudes from the surface of mature virions in three distinct environments, and docking studies predict Fab binding will leave five-fold clustered epitopes exposed. We also show that E16 inhibits infection primarily at a step after viral attachment, potentially by blocking envelope glycoprotein conformational changes. Collectively, our results suggest that a vaccine strategy targeting the dominant DIII epitope may elicit safe and effective immune responses against flaviviral diseases.

Structural basis of West Nile virus neutralization by a therapeutic antibody.,Nybakken GE, Oliphant T, Johnson S, Burke S, Diamond MS, Fremont DH Nature. 2005 Sep 29;437(7059):764-9. PMID:16193056^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nybakken GE, Oliphant T, Johnson S, Burke S, Diamond MS, Fremont DH. Structural basis of West Nile virus neutralization by a therapeutic antibody. Nature. 2005 Sep 29;437(7059):764-9. PMID:16193056 doi:10.1038/nature03956

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ztx"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ztx' size='340' side='right'caption='[[1ztx]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ztx]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Wnv Wnv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZTX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZTX FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ztx]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [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=1ZTX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZTX 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=1ztx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ztx OCA], [http://pdbe.org/1ztx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ztx RCSB], [http://www.ebi.ac.uk/pdbsum/1ztx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ztx ProSAT]</span></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]] 2.5&#8491;</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=1ztx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ztx OCA], [https://pdbe.org/1ztx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ztx RCSB], [https://www.ebi.ac.uk/pdbsum/1ztx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ztx ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/Q91KZ4_WNV Q91KZ4_WNV]
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 11: / Line 14: @@
   <jmolCheckbox>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zt/1ztx_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
@@ Line 34: / Line 37: @@
 [[Category: Large Structures]]
 [[Category: Mus musculus]]
-[[Category: Wnv]]
+[[Category: West Nile virus]]
-[[Category: Diamond, M S]]
+[[Category: Diamond MS]]
-[[Category: Fremont, D H]]
+[[Category: Fremont DH]]
-[[Category: Nybakken, G E]]
+[[Category: Nybakken GE]]
-[[Category: Oliphant, T]]
+[[Category: Oliphant T]]
-[[Category: Antibody]]
-[[Category: Envelope]]
-[[Category: Fab]]
-[[Category: Neutralizing]]
-[[Category: Viral protein-immune system complex]]
-[[Category: Virus]]

1ztx

From Proteopedia

Current revision

West Nile Virus Envelope Protein DIII in complex with neutralizing E16 antibody Fab

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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