View source for 1wdg


==crystal structure of MHV spike protein fusion core==
<StructureSection load='1wdg' size='340' side='right'caption='[[1wdg]], [[Resolution|resolution]] 2.06&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1wdg]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Cvma5 Cvma5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WDG FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1wdf|1wdf]]</div></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=1wdg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wdg OCA], [https://pdbe.org/1wdg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wdg RCSB], [https://www.ebi.ac.uk/pdbsum/1wdg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wdg ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/SPIKE_CVMA5 SPIKE_CVMA5]] S1 attaches the virion to the cell membrane by interacting with murine CEACAM1, initiating the infection.<ref>PMID:16014947</ref>   S2 is a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Presumably interacts with target cell lipid raft after cell attachment.<ref>PMID:16014947</ref>  
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/wd/1wdg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1wdg ConSurf].
<div style="clear:both"></div>
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== Publication Abstract from PubMed ==
The surface transmembrane glycoprotein is responsible for mediating virion attachment to cell and subsequent virus-cell membrane fusion. However, the molecular mechanisms for the viral entry of coronaviruses remain poorly understood. The crystal structure of the fusion core of mouse hepatitis virus S protein, which represents the first fusion core structure of any coronavirus, reveals a central hydrophobic coiled coil trimer surrounded by three helices in an oblique, antiparallel manner. This structure shares significant similarity with both the low pH-induced conformation of influenza hemagglutinin and fusion core of HIV gp41, indicating that the structure represents a fusion-active state formed after several conformational changes. Our results also indicate that the mechanisms for the viral fusion of coronaviruses are similar to those of influenza virus and HIV. The coiled coil structure has unique features, which are different from other viral fusion cores. Highly conserved heptad repeat 1 (HR1) and HR2 regions in coronavirus spike proteins indicate a similar three-dimensional structure among these fusion cores and common mechanisms for the viral fusion. We have proposed the binding regions of HR1 and HR2 of other coronaviruses and a structure model of their fusion core based on our mouse hepatitis virus fusion core structure and sequence alignment. Drug discovery strategies aimed at inhibiting viral entry by blocking hairpin formation may be applied to the inhibition of a number of emerging infectious diseases, including severe acute respiratory syndrome.

Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core.,Xu Y, Liu Y, Lou Z, Qin L, Li X, Bai Z, Pang H, Tien P, Gao GF, Rao Z J Biol Chem. 2004 Jul 16;279(29):30514-22. Epub 2004 Apr 27. PMID:15123674<ref>PMID:15123674</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 1wdg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Sandbox 3001|Sandbox 3001]]
*[[Spike protein|Spike protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Cvma5]]
[[Category: Large Structures]]
[[Category: Bai, Z]]
[[Category: Gao, G F]]
[[Category: Li, X]]
[[Category: Liu, Y]]
[[Category: Lou, Z]]
[[Category: Qin, L]]
[[Category: Rao, Z]]
[[Category: Tien, P]]
[[Category: Xu, Y]]
[[Category: Coronavirus]]
[[Category: Fusion core]]
[[Category: Heptad repeat]]
[[Category: Mhv]]
[[Category: Viral entry]]
[[Category: Viral protein]]