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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The threat of a major coronavirus pandemic urges the development of strategies to combat these pathogens. Human coronavirus NL63 (HCoV-NL63) is an alpha-coronavirus that can cause severe lower-respiratory-tract infections requiring hospitalization. We report here the 3.4-A-resolution cryo-EM reconstruction of the HCoV-NL63 coronavirus spike glycoprotein trimer, which mediates entry into host cells and is the main target of neutralizing antibodies during infection. The map resolves the extensive glycan shield obstructing the protein surface and, in combination with mass spectrometry, provides a structural framework to understand the accessibility to antibodies. The structure reveals the complete architecture of the fusion machinery including the triggering loop and the C-terminal domains, which contribute to anchoring the trimer to the viral membrane. Our data further suggest that HCoV-NL63 and other coronaviruses use molecular trickery, based on epitope masking with glycans and activating conformational changes, to evade the immune system of infected hosts.
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Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy.,Walls AC, Tortorici MA, Frenz B, Snijder J, Li W, Rey FA, DiMaio F, Bosch BJ, Veesler D Nat Struct Mol Biol. 2016 Sep 12. doi: 10.1038/nsmb.3293. PMID:27617430<ref>PMID:27617430</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5szs" style="background-color:#fffaf0;"></div>
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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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== References ==
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*[[Spike protein 3D structures|Spike protein 3D structures]]
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<references/>
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__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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Revision as of 15:34, 6 March 2024

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

5szs, resolution 3.40Å

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