6crz: Difference between revisions
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==SARS Spike Glycoprotein, Trypsin-cleaved, Stabilized variant, C3 symmetry== | |||
<StructureSection load='6crz' size='340' side='right' caption='[[6crz]], [[Resolution|resolution]] 3.30Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6crz]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CRZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CRZ FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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> | |||
[[Category: | <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=6crz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6crz OCA], [http://pdbe.org/6crz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6crz RCSB], [http://www.ebi.ac.uk/pdbsum/6crz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6crz ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[[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. | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Cottrell, C A]] | |||
[[Category: Kirchdoerfer, R N]] | |||
[[Category: McLellan, J S]] | |||
[[Category: Pallesen, J]] | |||
[[Category: Turner, H L]] | |||
[[Category: Wang, N]] | |||
[[Category: Ward, A B]] | |||
[[Category: Glycoprotein]] | |||
[[Category: Membrane fusion]] | |||
[[Category: Receptor binding]] | |||
[[Category: Viral protein]] | |||
Revision as of 13:54, 11 April 2018
SARS Spike Glycoprotein, Trypsin-cleaved, Stabilized variant, C3 symmetry
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