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<SX load='3ixx' size='340' side='right' viewer='molstar' caption='[[3ixx]], [[Resolution|resolution]] 15.00&Aring;' scene=''>
<SX load='3ixx' size='340' side='right' viewer='molstar' caption='[[3ixx]], [[Resolution|resolution]] 15.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3ixx]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [https://en.wikipedia.org/wiki/Wnv Wnv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3IXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IXX FirstGlance]. <br>
<table><tr><td colspan='2'>[[3ixx]] is a 10 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=3IXX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IXX FirstGlance]. <br>
</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=3ixx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ixx OCA], [https://pdbe.org/3ixx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ixx RCSB], [https://www.ebi.ac.uk/pdbsum/3ixx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ixx ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 15&#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=3ixx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ixx OCA], [https://pdbe.org/3ixx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ixx RCSB], [https://www.ebi.ac.uk/pdbsum/3ixx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ixx ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/Q9Q6P4_WNV Q9Q6P4_WNV]] 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:SAAS011998_004_099774] [[https://www.uniprot.org/uniprot/Q9WHD2_WNV Q9WHD2_WNV]] 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:SAAS026470_004_099774]  
[https://www.uniprot.org/uniprot/A7TZT4_WNV A7TZT4_WNV] Functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter.[ARBA:ARBA00003504] Serine protease subunit NS2B: Required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ixx ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ixx ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Flaviviruses are a group of human pathogens causing severe encephalitic or hemorrhagic diseases that include West Nile, dengue and yellow fever viruses. Here, using X-ray crystallography we have defined the structure of the flavivirus cross-reactive antibody E53 that engages the highly conserved fusion loop of the West Nile virus envelope glycoprotein. Using cryo-electron microscopy, we also determined that E53 Fab binds preferentially to spikes in noninfectious, immature flavivirions but is unable to bind significantly to mature virions, consistent with the limited solvent exposure of the epitope. We conclude that the neutralizing impact of E53 and likely similar fusion-loop-specific antibodies depends on its binding to the frequently observed immature component of flavivirus particles. Our results elucidate how fusion-loop antibodies, which comprise a significant fraction of the humoral response against flaviviruses, can function to control infection without appreciably recognizing mature virions. As these highly cross-reactive antibodies are often weakly neutralizing they also may contribute to antibody-dependent enhancement and flavi virus pathogenesis thereby complicating development of safe and effective vaccines.
Structural basis for the preferential recognition of immature flaviviruses by a fusion-loop antibody.,Cherrier MV, Kaufmann B, Nybakken GE, Lok SM, Warren JT, Chen BR, Nelson CA, Kostyuchenko VA, Holdaway HA, Chipman PR, Kuhn RJ, Diamond MS, Rossmann MG, Fremont DH EMBO J. 2009 Oct 21;28(20):3269-76. Epub 2009 Aug 27. PMID:19713934<ref>PMID:19713934</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3ixx" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Antibody 3D structures|Antibody 3D structures]]
*[[Antibody 3D structures|Antibody 3D structures]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Lk3 transgenic mice]]
[[Category: Mus musculus]]
[[Category: Wnv]]
[[Category: West Nile virus]]
[[Category: Cherrier, M V]]
[[Category: Cherrier MV]]
[[Category: Chipman, P R]]
[[Category: Chipman PR]]
[[Category: Diamond, M S]]
[[Category: Diamond MS]]
[[Category: Fremont, D H]]
[[Category: Fremont DH]]
[[Category: Holdaway, H A]]
[[Category: Holdaway HA]]
[[Category: Kaufmann, B]]
[[Category: Kaufmann B]]
[[Category: Kostyuchenko, V A]]
[[Category: Kostyuchenko VA]]
[[Category: Kuhn, R J]]
[[Category: Kuhn RJ]]
[[Category: Lok, S M]]
[[Category: Lok SM]]
[[Category: Nelson, C A]]
[[Category: Nelson CA]]
[[Category: Nybakken, G E]]
[[Category: Nybakken GE]]
[[Category: Rossmann, M G]]
[[Category: Rossmann MG]]
[[Category: Warren, J T]]
[[Category: Warren JT]]
[[Category: Atp-binding]]
[[Category: E53]]
[[Category: Envelope protein]]
[[Category: Fab]]
[[Category: Fusion loop]]
[[Category: Helicase]]
[[Category: Hydrolase]]
[[Category: Icosahedral virus]]
[[Category: Immature]]
[[Category: Membrane]]
[[Category: Nucleotide-binding]]
[[Category: Rna replication]]
[[Category: Transmembrane]]
[[Category: Virion]]
[[Category: Virus]]
[[Category: West nile virus]]

Latest revision as of 10:07, 21 February 2024

The pseudo-atomic structure of West Nile immature virus in complex with Fab fragments of the anti-fusion loop antibody E53

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