8do4
From Proteopedia
(Difference between revisions)
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- | '''Unreleased structure''' | ||
- | + | ==Prefusion-stabilized Nipah virus fusion protein, dimer of trimers== | |
- | + | <StructureSection load='8do4' size='340' side='right'caption='[[8do4]], [[Resolution|resolution]] 3.20Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[8do4]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Nipah_henipavirus Nipah henipavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8DO4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8DO4 FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.2Å</td></tr> | |
- | [[Category: | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8do4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8do4 OCA], [https://pdbe.org/8do4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8do4 RCSB], [https://www.ebi.ac.uk/pdbsum/8do4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8do4 ProSAT]</span></td></tr> |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/FUS_NIPAV FUS_NIPAV] Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions 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 plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity). | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
+ | [[Category: Nipah henipavirus]] | ||
+ | [[Category: Blade EG]] | ||
+ | [[Category: Byrne PO]] | ||
+ | [[Category: McLellan JS]] |
Revision as of 06:12, 19 July 2023
Prefusion-stabilized Nipah virus fusion protein, dimer of trimers
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