1jek
From Proteopedia
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{{STRUCTURE_1jek| PDB=1jek | SCENE= }} | {{STRUCTURE_1jek| PDB=1jek | SCENE= }} | ||
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===Visna TM CORE STRUCTURE=== | ===Visna TM CORE STRUCTURE=== | ||
+ | {{ABSTRACT_PUBMED_11447278}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/ENV_VILVK ENV_VILVK]] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). The transmembrane protein (TM) acts as a 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 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. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity). | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:011447278</ref><references group="xtra"/> | + | <ref group="xtra">PMID:011447278</ref><references group="xtra"/><references/> |
[[Category: Kim, P S.]] | [[Category: Kim, P S.]] | ||
[[Category: Malashkevich, V N.]] | [[Category: Malashkevich, V N.]] |
Revision as of 10:33, 16 April 2014
Contents |
Visna TM CORE STRUCTURE
Template:ABSTRACT PUBMED 11447278
Function
[ENV_VILVK] The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity). The transmembrane protein (TM) acts as a 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 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. Membranes fusion leads to delivery of the nucleocapsid into the cytoplasm (By similarity).
About this Structure
1jek is a 2 chain structure. Full crystallographic information is available from OCA.
Reference
- Malashkevich VN, Singh M, Kim PS. The trimer-of-hairpins motif in membrane fusion: Visna virus. Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8502-6. Epub 2001 Jul 10. PMID:11447278 doi:10.1073/pnas.151254798
Categories: Kim, P S. | Malashkevich, V N. | Singh, M. | Envelope glycoprotein | Gp41 | Hiv | Retrovirus | Siv | Viral protein