1wp7

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==crystal structure of Nipah Virus fusion core==
==crystal structure of Nipah Virus fusion core==
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<StructureSection load='1wp7' size='340' side='right' caption='[[1wp7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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<StructureSection load='1wp7' size='340' side='right'caption='[[1wp7]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1wp7]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Nipav Nipav]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WP7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WP7 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1wp7]] is a 3 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=1WP7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WP7 FirstGlance]. <br>
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</td></tr><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=1wp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wp7 OCA], [http://pdbe.org/1wp7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wp7 RCSB], [http://www.ebi.ac.uk/pdbsum/1wp7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wp7 ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wp7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wp7 OCA], [https://pdbe.org/1wp7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wp7 RCSB], [https://www.ebi.ac.uk/pdbsum/1wp7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wp7 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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).
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[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>
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[[Category: Nipav]]
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[[Category: Large Structures]]
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[[Category: Bai, Z]]
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[[Category: Nipah henipavirus]]
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[[Category: Gao, G F]]
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[[Category: Bai Z]]
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[[Category: Liu, Y]]
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[[Category: Gao GF]]
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[[Category: Lou, Z]]
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[[Category: Liu Y]]
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[[Category: Rao, Z]]
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[[Category: Lou Z]]
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[[Category: Su, N]]
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[[Category: Rao Z]]
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[[Category: Xu, Y]]
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[[Category: Su N]]
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[[Category: Fusion core]]
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[[Category: Xu Y]]
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[[Category: Heptad repeat]]
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[[Category: Nipah virus]]
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[[Category: Viral protein]]
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Current revision

crystal structure of Nipah Virus fusion core

PDB ID 1wp7

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