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

@article{Murphy2017SolutionSA,
  title={Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.},
  author={R Elliot Murphy and Alexandra B. Samal and Jiř{\'i} Vlach and Jamil S Saad},
  journal={Structure},
  year={2017},
  volume={25 11},
  pages={
          1708-1718.e5
        }
}
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… CONTINUE READING
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