6c6y: Difference between revisions

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 <StructureSection load='6c6y' size='340' side='right'caption='[[6c6y]], [[Resolution|resolution]] 3.32&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6c6y]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Betacoronavirus_england_1 Betacoronavirus england 1] and [http://en.wikipedia.org/wiki/Macmu Macmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C6Y OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C6Y FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6c6y]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Betacoronavirus_England_1 Betacoronavirus England 1] and [https://en.wikipedia.org/wiki/Macaca_mulatta Macaca mulatta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6C6Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C6Y FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 3.32&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S, 3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1263720 Betacoronavirus England 1])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<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=6c6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c6y OCA], [http://pdbe.org/6c6y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c6y RCSB], [http://www.ebi.ac.uk/pdbsum/6c6y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c6y 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=6c6y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c6y OCA], [https://pdbe.org/6c6y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c6y RCSB], [https://www.ebi.ac.uk/pdbsum/6c6y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c6y ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SPIKE_CVEMC SPIKE_CVEMC]] S1 attaches the virion to the cell membrane by interacting with host DPP4, initiating the infection.<ref>PMID:23486063</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 (By similarity).
+[https://www.uniprot.org/uniprot/SPIKE_MERS1 SPIKE_MERS1] Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Interacts with host DPP4 to mediate virla entry.[HAMAP-Rule:MF_04099]<ref>PMID:23486063</ref>   Mediates fusion of the virion and cellular membranes by acting as 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.[HAMAP-Rule:MF_04099]  Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
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 </div>
 <div class="pdbe-citations 6c6y" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Sandbox 3001|Sandbox 3001]]
+*[[Spike protein 3D structures|Spike protein 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Betacoronavirus england 1]]
+[[Category: Betacoronavirus England 1]]
 [[Category: Large Structures]]
-[[Category: Macmu]]
+[[Category: Macaca mulatta]]
-[[Category: Graham, B S]]
+[[Category: Graham BS]]
-[[Category: Joyce, M G]]
+[[Category: Joyce MG]]
-[[Category: Kwong, P D]]
+[[Category: Kwong PD]]
-[[Category: Mascola, J R]]
+[[Category: Mascola JR]]
-[[Category: Antibody]]
-[[Category: Immune system]]
-[[Category: Neutralizing]]
-[[Category: Vaccine]]