7n1v

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (11:36, 30 October 2024) (edit) (undo)
 
Line 3: Line 3:
<StructureSection load='7n1v' size='340' side='right'caption='[[7n1v]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
<StructureSection load='7n1v' size='340' side='right'caption='[[7n1v]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[7n1v]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/2019-ncov 2019-ncov]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N1V FirstGlance]. <br>
+
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7N1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7N1V FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.5&#8491;</td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S, 2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2697049 2019-nCoV])</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7n1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n1v OCA], [https://pdbe.org/7n1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n1v RCSB], [https://www.ebi.ac.uk/pdbsum/7n1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n1v ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7n1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7n1v OCA], [https://pdbe.org/7n1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7n1v RCSB], [https://www.ebi.ac.uk/pdbsum/7n1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7n1v ProSAT]</span></td></tr>
</table>
</table>
-
== Function ==
 
-
[[https://www.uniprot.org/uniprot/SPIKE_SARS2 SPIKE_SARS2]] attaches the virion to the cell membrane by interacting with host receptor, initiating the infection (By similarity). Binding to human ACE2 receptor and internalization of the virus into the endosomes of the host cell induces conformational changes in the Spike glycoprotein (PubMed:32142651, PubMed:32075877, PubMed:32155444). Uses also human TMPRSS2 for priming in human lung cells which is an essential step for viral entry (PubMed:32142651). Proteolysis by cathepsin CTSL may unmask the fusion peptide of S2 and activate membranes fusion within endosomes.[HAMAP-Rule:MF_04099]<ref>PMID:32075877</ref> <ref>PMID:32142651</ref> <ref>PMID:32155444</ref> mediates fusion of the virion and cellular membranes by acting as 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.[HAMAP-Rule:MF_04099] Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099]
 
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Line 23: Line 21:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: 2019-ncov]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Cai, Y F]]
+
[[Category: Cai YF]]
-
[[Category: Chen, B]]
+
[[Category: Chen B]]
-
[[Category: Jr, R M.Walsh]]
+
[[Category: Peng HQ]]
-
[[Category: Peng, H Q]]
+
[[Category: Rawson S]]
-
[[Category: Rawson, S]]
+
[[Category: Sterling SM]]
-
[[Category: Sterling, S M]]
+
[[Category: Volloch SR]]
-
[[Category: Volloch, S R]]
+
[[Category: Walsh Jr RM]]
-
[[Category: Xiao, T S]]
+
[[Category: Xiao TS]]
-
[[Category: Zhang, J]]
+
[[Category: Zhang J]]
-
[[Category: Viral protein]]
+

Current revision

Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variants

PDB ID 7n1v

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools