4jf3

From Proteopedia

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Template:STRUCTURE 4jf3

Contents 1 Crystal structure of the mpmv tm retroviral fusion core 2 Function 3 About this Structure 4 Reference

Crystal structure of the mpmv tm retroviral fusion core

Template:ABSTRACT PUBMED 24131724

Function

[ENV_MPMV] 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

4jf3 is a 2 chain structure with sequence from Mpmv. Full crystallographic information is available from OCA.

Reference

• Aydin H, Cook JD, Lee JE. Crystal structures of Beta- and gammaretrovirus fusion proteins reveal a role for electrostatic stapling in viral entry. J Virol. 2014 Jan;88(1):143-53. doi: 10.1128/JVI.02023-13. Epub 2013 Oct 16. PMID:24131724 doi:http://dx.doi.org/10.1128/JVI.02023-13