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Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.

Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.
Author Information (click to view)

Murphy RE, Samal AB, Vlach J, Saad JS,


Murphy RE, Samal AB, Vlach J, Saad JS, (click to view)

Murphy RE, Samal AB, Vlach J, Saad JS,

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Structure (London, England : 1993) 2017 10 1925(11) 1708-1718.e5 pii 10.1016/j.str.2017.09.010

Abstract

The cytoplasmic tail of gp41 (gp41CT) remains the last HIV-1 domain with an unknown structure. It plays important roles in HIV-1 replication such as mediating envelope (Env) intracellular trafficking and incorporation into assembling virions, mechanisms of which are poorly understood. Here, we present the solution structure of gp41CT in a micellar environment and characterize its interaction with the membrane. We show that the N-terminal 45 residues are unstructured and not associated with the membrane. However, the C-terminal 105 residues form three membrane-bound amphipathic α helices with distinctive structural features such as variable degree of membrane penetration, hydrophobic and basic surfaces, clusters of aromatic residues, and a network of cation-π interactions. This work fills a major gap by providing the structure of the last segment of HIV-1 Env, which will provide insights into the mechanisms of Gag-mediated Env incorporation as well as the overall Env mobility and conformation on the virion surface.

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