1zvb

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==A structure-based mechanism of SARS virus membrane fusion==
==A structure-based mechanism of SARS virus membrane fusion==
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<StructureSection load='1zvb' size='340' side='right' caption='[[1zvb]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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<StructureSection load='1zvb' size='340' side='right'caption='[[1zvb]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1zvb]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvhsa Cvhsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZVB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZVB FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1zvb]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cvhsa Cvhsa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZVB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZVB FirstGlance]. <br>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1zv7|1zv7]], [[1zv8|1zv8]], [[1zva|1zva]]</td></tr>
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1zv7|1zv7]], [[1zv8|1zv8]], [[1zva|1zva]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 CVHSA])</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=227859 CVHSA])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zvb OCA], [http://pdbe.org/1zvb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zvb RCSB], [http://www.ebi.ac.uk/pdbsum/1zvb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zvb ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zvb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zvb OCA], [https://pdbe.org/1zvb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zvb RCSB], [https://www.ebi.ac.uk/pdbsum/1zvb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zvb ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SPIKE_CVHSA SPIKE_CVHSA]] S1 attaches the virion to the cell membrane by interacting with human ACE2 and CLEC4M/DC-SIGNR, initiating the infection. Binding to the receptor and internalization of the virus into the endosomes of the host cell probably induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes. S2 is a class I viral fusion protein. Under the current model, the protein has at least three 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 target cell membranes.
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[[https://www.uniprot.org/uniprot/SPIKE_CVHSA SPIKE_CVHSA]] S1 attaches the virion to the cell membrane by interacting with human ACE2 and CLEC4M/DC-SIGNR, initiating the infection. Binding to the receptor and internalization of the virus into the endosomes of the host cell probably induces conformational changes in the S glycoprotein. Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes. S2 is a class I viral fusion protein. Under the current model, the protein has at least three 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 target cell membranes.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</div>
</div>
<div class="pdbe-citations 1zvb" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 1zvb" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Sandbox 3001|Sandbox 3001]]
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*[[Spike protein|Spike protein]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Cvhsa]]
[[Category: Cvhsa]]
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[[Category: Large Structures]]
[[Category: Dai, J]]
[[Category: Dai, J]]
[[Category: Deng, Y]]
[[Category: Deng, Y]]

Revision as of 08:17, 27 January 2021

A structure-based mechanism of SARS virus membrane fusion

PDB ID 1zvb

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