3n27: Difference between revisions

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<StructureSection load='3n27' size='340' side='right'caption='[[3n27]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3n27' size='340' side='right'caption='[[3n27]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3n27]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N27 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3n27]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Hendra_henipavirus Hendra henipavirus] and [https://en.wikipedia.org/wiki/Nipah_henipavirus Nipah henipavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N27 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3N27 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=TBU:TERTIARY-BUTYL+ALCOHOL'>TBU</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=3n27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n27 OCA], [https://pdbe.org/3n27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n27 RCSB], [https://www.ebi.ac.uk/pdbsum/3n27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n27 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=3n27 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3n27 OCA], [https://pdbe.org/3n27 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3n27 RCSB], [https://www.ebi.ac.uk/pdbsum/3n27 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3n27 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== 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).  
[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__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Hendra henipavirus]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Liu, J]]
[[Category: Nipah henipavirus]]
[[Category: Lu, M]]
[[Category: Liu J]]
[[Category: Antivirus agent]]
[[Category: Lu M]]
[[Category: Chimera protein]]
[[Category: Fusion inhibitor]]
[[Category: Fusion protein]]
[[Category: Viral protein]]

Latest revision as of 09:07, 6 September 2023

Molecular Basis of the Inhibition of Henipa Viruses

3n27, resolution 1.80Å

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