5szs

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<SX load='5szs' size='340' side='right' viewer='molstar' caption='[[5szs]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<SX load='5szs' size='340' side='right' viewer='molstar' caption='[[5szs]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5szs]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Cvhnl Cvhnl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SZS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5SZS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5szs]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_coronavirus_NL63 Human coronavirus NL63]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SZS FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S, 2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=277944 CVHNL])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5szs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5szs OCA], [http://pdbe.org/5szs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5szs RCSB], [http://www.ebi.ac.uk/pdbsum/5szs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5szs 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=5szs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5szs OCA], [https://pdbe.org/5szs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5szs RCSB], [https://www.ebi.ac.uk/pdbsum/5szs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5szs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SPIKE_CVHNL SPIKE_CVHNL]] S1 region attaches the virion to the cell membrane by interacting with human ACE2, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the 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) regions 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 (By similarity).
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[https://www.uniprot.org/uniprot/SPIKE_CVHNL SPIKE_CVHNL] S1 region attaches the virion to the cell membrane by interacting with human ACE2, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to the 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) regions 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 (By similarity).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
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*[[Spike protein|Spike protein]]
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*[[Sandbox 3001|Sandbox 3001]]
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*[[Spike protein 3D structures|Spike protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</SX>
</SX>
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[[Category: Cvhnl]]
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[[Category: Human coronavirus NL63]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bosch, B J]]
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[[Category: Bosch BJ]]
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[[Category: DiMaio, F]]
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[[Category: DiMaio F]]
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[[Category: Frenz, B]]
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[[Category: Frenz B]]
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[[Category: Li, W]]
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[[Category: Li W]]
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[[Category: Rey, F A]]
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[[Category: Rey FA]]
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[[Category: Snijder, J]]
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[[Category: Snijder J]]
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[[Category: Tortorici, M A]]
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[[Category: Tortorici MA]]
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[[Category: Veesler, D]]
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[[Category: Veesler D]]
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[[Category: Walls, A C]]
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[[Category: Walls AC]]
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[[Category: Coronavirus]]
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[[Category: Nl63]]
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[[Category: Vaccine]]
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[[Category: Viral fusion protein]]
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[[Category: Viral protein]]
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Current revision

Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy

5szs, resolution 3.40Å

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