7v6o: Difference between revisions

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'''Unreleased structure'''


The entry 7v6o is ON HOLD until Paper Publication
==MERS S ectodomain trimer in complex with neutralizing antibody 111 (state 2)==
 
<StructureSection load='7v6o' size='340' side='right'caption='[[7v6o]], [[Resolution|resolution]] 4.56&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[7v6o]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_betacoronavirus_2c_EMC/2012 Human betacoronavirus 2c EMC/2012]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7V6O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V6O FirstGlance]. <br>
Description:  
</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=7v6o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v6o OCA], [https://pdbe.org/7v6o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v6o RCSB], [https://www.ebi.ac.uk/pdbsum/7v6o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v6o ProSAT]</span></td></tr>
[[Category: Unreleased Structures]]
</table>
== Function ==
[[https://www.uniprot.org/uniprot/K0BRG7_MERS K0BRG7_MERS]] Spike protein S1: attaches the virion to the cell membrane by interacting with host receptor, initiating the infection.[HAMAP-Rule:MF_04099]  Spike protein S2': Acts as a viral fusion peptide which is unmasked following S2 cleavage occurring upon virus endocytosis.[HAMAP-Rule:MF_04099] Spike protein S2: 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]
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Human betacoronavirus 2c EMC/2012]]
[[Category: Large Structures]]
[[Category: Wang X]]
[[Category: Wang Y]]
[[Category: Wang Z]]
[[Category: Zeng J]]
[[Category: Zhang S]]
[[Category: Zhao J]]