6crv: Difference between revisions

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-'''Unreleased structure'''
-The entry 6crv is ON HOLD
+==SARS Spike Glycoprotein, Stabilized variant, C3 symmetry==
+<StructureSection load='6crv' size='340' side='right' caption='[[6crv]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
-Authors:
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6crv]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CRV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6CRV FirstGlance]. <br>
-Description:
+</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=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-[[Category: Unreleased Structures]]
+<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=6crv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6crv OCA], [http://pdbe.org/6crv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6crv RCSB], [http://www.ebi.ac.uk/pdbsum/6crv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6crv 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]]