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4jgs
From Proteopedia
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| - | + | {{STRUCTURE_4jgs| PDB=4jgs | SCENE= }} | |
| + | ===Crystal structure of the xmrv tm retroviral fusion core=== | ||
| - | The | + | ==Function== |
| + | [[http://www.uniprot.org/uniprot/ENV1_MOUSE ENV1_MOUSE]] 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== | |
| - | + | [[4jgs]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JGS OCA]. | |
| - | + | [[Category: Mus musculus]] | |
| + | [[Category: Aydin, H.]] | ||
| + | [[Category: Cook, J D.]] | ||
| + | [[Category: Lee, J E.]] | ||
| + | [[Category: Six helix bundle]] | ||
| + | [[Category: Viral protein]] | ||
| + | [[Category: Viral surface]] | ||
| + | [[Category: Viral-host membrane fusion]] | ||
| + | [[Category: Xmrv tm]] | ||
Revision as of 06:53, 23 October 2013
Crystal structure of the xmrv tm retroviral fusion core
Function
[ENV1_MOUSE] 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
4jgs is a 9 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA.
