4jpr
Structure of the ASLV fusion subunit coreStructure of the ASLV fusion subunit core
Template:ABSTRACT PUBMED 24036886
FunctionFunction
[ENV_RSVSA] 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 StructureAbout this Structure
4jpr is a 1 chain structure with sequence from Rous sarcoma virus (strain schmidt-ruppin a). Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Aydin H, Smrke BM, Lee JE. Structural characterization of a fusion glycoprotein from a retrovirus that undergoes a hybrid 2-step entry mechanism. FASEB J. 2013 Sep 13. PMID:24036886 doi:10.1096/fj.13-232371