3n27
From Proteopedia
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{{STRUCTURE_3n27| PDB=3n27 | SCENE= }} | {{STRUCTURE_3n27| PDB=3n27 | SCENE= }} | ||
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===Molecular Basis of the Inhibition of Henipa Viruses=== | ===Molecular Basis of the Inhibition of Henipa Viruses=== | ||
| + | ==Function== | ||
| + | [[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). | ||
==About this Structure== | ==About this Structure== | ||
| - | [[3n27]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/ | + | [[3n27]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Nipah_virus Nipah virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3N27 OCA]. |
| - | [[Category: | + | [[Category: Nipah virus]] |
[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
[[Category: Lu, M.]] | [[Category: Lu, M.]] | ||
Revision as of 08:30, 2 May 2013
Molecular Basis of the Inhibition of Henipa Viruses
Function
[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).
About this Structure
3n27 is a 3 chain structure with sequence from Nipah virus. Full crystallographic information is available from OCA.
