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Publication Abstract from PubMed

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 alpha 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-pi 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.

Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.,Murphy RE, Samal AB, Vlach J, Saad JS Structure. 2017 Oct 13. pii: S0969-2126(17)30301-5. doi:, 10.1016/j.str.2017.09.010. PMID:29056482^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.