View source for 5mdm


==Structural intermediates in the fusion associated transition of vesiculovirus glycoprotein==
<StructureSection load='5mdm' size='340' side='right'caption='[[5mdm]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mdm]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Chandipura_virus Chandipura virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MDM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MDM 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]] 2.998&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5mdm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mdm OCA], [https://pdbe.org/5mdm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mdm RCSB], [https://www.ebi.ac.uk/pdbsum/5mdm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mdm ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLYCO_CHAV GLYCO_CHAV] Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Vesiculoviruses enter cells by membrane fusion, driven by a large, low-pH-induced, conformational change in the fusion glycoprotein G that involves transition from a trimeric pre-fusion toward a trimeric post-fusion state via monomeric intermediates. Here, we present the structure of the G fusion protein at intermediate pH for two vesiculoviruses, vesicular stomatitis virus (VSV) and Chandipura virus (CHAV), which is responsible for deadly encephalopathies. First, a CHAV G crystal structure shows two intermediate conformations forming a flat dimer of heterodimers. On virions, electron microscopy (EM) and tomography reveal monomeric spikes similar to one of the crystal conformations. In solution, mass spectrometry shows dimers of G. Finally, mutations at a dimer interface, involving fusion domains associated in an antiparallel manner to form an intermolecular beta-sheet, affect G fusion properties. The location of the compensatory mutations restoring fusion activity strongly suggests that this interface is functionally relevant. This work reveals the range of G structural changes and suggests that G monomers can re-associate, through antiparallel interactions between fusion domains, into dimers that play a role at some early stage of the fusion process.

Structural intermediates in the fusion-associated transition of vesiculovirus glycoprotein.,Baquero E, Albertini AA, Raux H, Abou-Hamdan A, Boeri-Erba E, Ouldali M, Buonocore L, Rose JK, Lepault J, Bressanelli S, Gaudin Y EMBO J. 2017 Mar 1;36(5):679-692. doi: 10.15252/embj.201694565. Epub 2017 Feb 10. PMID:28188244<ref>PMID:28188244</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5mdm" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chandipura virus]]
[[Category: Large Structures]]
[[Category: Albertini AA]]
[[Category: Baquero E]]
[[Category: Bressanelli S]]
[[Category: Gaudin Y]]