5VWL

Solution NMR Structure of the Membrane Associated Segment of HIV-1 gp41 Cytoplasmic Tail

Summary for 5VWL

• Entry DOI: 10.2210/pdb5vwl/pdb
• NMR Information: BMRB: 30297
• Descriptor: Cytoplasmic tail of HIV-1 gp41 protein (1 entity in total)
• Functional Keywords: alpha-helix, cytoplasmic tail, hiv-1, envelope, plasma membrane, viral protein
• Biological source: Human immunodeficiency virus 1
• Total number of polymer chains: 1
• Total formula weight: 12398.52

Authors

Saad, J.S.,Murphy, R.E.,Samal, A.,Vlach, J. (deposition date: 2017-05-22, release date: 2017-11-08, Last modification date: 2024-05-15)

Primary citation

Murphy, R.E.,Samal, A.B.,Vlach, J.,Saad, J.S.
Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein.
Structure, 25:1708-1718.e5, 2017

PubMed 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.

PubMed: 29056482
DOI: 10.1016/j.str.2017.09.010

Experimental method

SOLUTION NMR