1wdf: Difference between revisions

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<StructureSection load='1wdf' size='340' side='right'caption='[[1wdf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1wdf' size='340' side='right'caption='[[1wdf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1wdf]] 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=1WDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WDF FirstGlance]. <br>
<table><tr><td colspan='2'>[[1wdf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Murine_hepatitis_virus_strain_A59 Murine hepatitis virus strain A59]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WDF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WDF 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;'>[[1wdg|1wdg]]</div></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=1wdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wdf OCA], [https://pdbe.org/1wdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wdf RCSB], [https://www.ebi.ac.uk/pdbsum/1wdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wdf ProSAT]</span></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=1wdf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wdf OCA], [https://pdbe.org/1wdf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wdf RCSB], [https://www.ebi.ac.uk/pdbsum/1wdf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wdf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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>
[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 ==
== 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=1wdf 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=1wdf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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>
</div>
<div class="pdbe-citations 1wdf" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Sandbox 3001|Sandbox 3001]]
*[[Sandbox 3001|Sandbox 3001]]
*[[Spike protein|Spike protein]]
*[[Spike protein 3D structures|Spike protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Cvma5]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Bai, Z]]
[[Category: Murine hepatitis virus strain A59]]
[[Category: Gao, G F]]
[[Category: Bai Z]]
[[Category: Li, X]]
[[Category: Gao GF]]
[[Category: Liu, Y]]
[[Category: Li X]]
[[Category: Lou, Z]]
[[Category: Liu Y]]
[[Category: Qin, L]]
[[Category: Lou Z]]
[[Category: Rao, Z]]
[[Category: Qin L]]
[[Category: Tien, P]]
[[Category: Rao Z]]
[[Category: Xu, Y]]
[[Category: Tien P]]
[[Category: Coronavirus]]
[[Category: Xu Y]]
[[Category: Fusion core]]
[[Category: Heptad repeat]]
[[Category: Mhv]]
[[Category: Viral entry]]
[[Category: Viral protein]]

Latest revision as of 16:31, 13 March 2024

crystal structure of MHV spike protein fusion corecrystal structure of MHV spike protein fusion core

Structural highlights

1wdf is a 2 chain structure with sequence from Murine hepatitis virus strain A59. 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

SPIKE_CVMA5 S1 attaches the virion to the cell membrane by interacting with murine CEACAM1, initiating the infection.[1] 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.[2]

Evolutionary Conservation

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

See Also

References

  1. ↑ Choi KS, Aizaki H, Lai MM. Murine coronavirus requires lipid rafts for virus entry and cell-cell fusion but not for virus release. J Virol. 2005 Aug;79(15):9862-71. PMID:16014947 doi:http://dx.doi.org/79/15/9862
  2. ↑ Choi KS, Aizaki H, Lai MM. Murine coronavirus requires lipid rafts for virus entry and cell-cell fusion but not for virus release. J Virol. 2005 Aug;79(15):9862-71. PMID:16014947 doi:http://dx.doi.org/79/15/9862

1wdf, resolution 2.50Å

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