6acd: Difference between revisions

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'''Unreleased structure'''


The entry 6acd is ON HOLD
==Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-free conformation with one RBD in up conformation==
 
<StructureSection load='6acd' size='340' side='right' caption='[[6acd]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
Authors: Gui, M., Song, W.
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6acd]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ACD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6ACD FirstGlance]. <br>
Description: Trypsin-cleaved and low pH-treated SARS-CoV spike glycoprotein and ACE2 complex, ACE2-free conformation with one RBD in up conformation
</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=6acd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6acd OCA], [http://pdbe.org/6acd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6acd RCSB], [http://www.ebi.ac.uk/pdbsum/6acd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6acd ProSAT]</span></td></tr>
[[Category: Unreleased Structures]]
</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: Gui, M]]
[[Category: Gui, M]]
[[Category: Song, W]]
[[Category: Song, W]]
[[Category: Class i fusion protein]]
[[Category: Glycoprotein]]
[[Category: Membrane fusion]]
[[Category: Sars-cov]]
[[Category: Spike]]
[[Category: Viral protein]]