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| | <SX load='3jcl' size='340' side='right' viewer='molstar' caption='[[3jcl]], [[Resolution|resolution]] 4.00Å' scene=''> | | <SX load='3jcl' size='340' side='right' viewer='molstar' caption='[[3jcl]], [[Resolution|resolution]] 4.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3jcl]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvma5 Cvma5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JCL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3JCL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3jcl]] is a 3 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=3JCL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3JCL FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">3, S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11142 CVMA5])</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]] 4Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3jcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jcl OCA], [http://pdbe.org/3jcl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jcl RCSB], [http://www.ebi.ac.uk/pdbsum/3jcl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jcl 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=3jcl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jcl OCA], [https://pdbe.org/3jcl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3jcl RCSB], [https://www.ebi.ac.uk/pdbsum/3jcl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3jcl ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| - | *[[Spike protein|Spike protein]] | + | *[[Sandbox 3001|Sandbox 3001]] |
| | + | *[[Spike protein 3D structures|Spike protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Cvma5]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bosch, B J]] | + | [[Category: Murine hepatitis virus strain A59]] |
| - | [[Category: DiMaio, F]] | + | [[Category: Bosch BJ]] |
| - | [[Category: Frenz, B]] | + | [[Category: DiMaio F]] |
| - | [[Category: Rey, F A]] | + | [[Category: Frenz B]] |
| - | [[Category: Rottier, P J.M]] | + | [[Category: Rey FA]] |
| - | [[Category: Tortorici, M A]] | + | [[Category: Rottier PJM]] |
| - | [[Category: Veesler, D]] | + | [[Category: Tortorici MA]] |
| - | [[Category: Walls, A C]] | + | [[Category: Veesler D]] |
| - | [[Category: Coronavirus]]
| + | [[Category: Walls AC]] |
| - | [[Category: Peplomer]]
| + | |
| - | [[Category: Viral fusion protein]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Viral spike]]
| + | |
| Structural highlights
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]
Publication Abstract from PubMed
The tremendous pandemic potential of coronaviruses was demonstrated twice in the past few decades by two global outbreaks of deadly pneumonia. Entry of coronaviruses into cells is mediated by the transmembrane spike glycoprotein S, which forms a trimer carrying receptor-binding and membrane fusion functions. S also contains the principal antigenic determinants and is the target of neutralizing antibodies. Here we present the structure of a mouse coronavirus S trimer ectodomain determined at 4.0 A resolution by single particle cryo-electron microscopy. It reveals the metastable pre-fusion architecture of S and highlights key interactions stabilizing it. The structure shares a common core with paramyxovirus F proteins, implicating mechanistic similarities and an evolutionary connection between these viral fusion proteins. The accessibility of the highly conserved fusion peptide at the periphery of the trimer indicates potential vaccinology strategies to elicit broadly neutralizing antibodies against coronaviruses. Finally, comparison with crystal structures of human coronavirus S domains allows rationalization of the molecular basis for species specificity based on the use of spatially contiguous but distinct domains.
Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer.,Walls AC, Tortorici MA, Bosch BJ, Frenz B, Rottier PJ, DiMaio F, Rey FA, Veesler D Nature. 2016 Feb 8. doi: 10.1038/nature16988. PMID:26855426[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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
- ↑ 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
- ↑ Walls AC, Tortorici MA, Bosch BJ, Frenz B, Rottier PJ, DiMaio F, Rey FA, Veesler D. Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer. Nature. 2016 Feb 8. doi: 10.1038/nature16988. PMID:26855426 doi:http://dx.doi.org/10.1038/nature16988
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