2fxp: Difference between revisions
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==Solution Structure of the SARS-Coronavirus HR2 Domain== | ==Solution Structure of the SARS-Coronavirus HR2 Domain== | ||
<StructureSection load='2fxp' size='340' side='right' caption='[[2fxp]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='2fxp' size='340' side='right'caption='[[2fxp]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2fxp]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2fxp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Cvhsa Cvhsa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FXP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FXP FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S ([ | </td></tr><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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2fxp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fxp OCA], [https://pdbe.org/2fxp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2fxp RCSB], [https://www.ebi.ac.uk/pdbsum/2fxp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2fxp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[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 2fxp" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2fxp" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Sandbox 3001|Sandbox 3001]] | |||
*[[Spike protein|Spike protein]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Cvhsa]] | [[Category: Cvhsa]] | ||
[[Category: Large Structures]] | |||
[[Category: Caffrey, M]] | [[Category: Caffrey, M]] | ||
[[Category: Hakansson-McReynolds, S]] | [[Category: Hakansson-McReynolds, S]] | ||