2N28

Solid-state NMR structure of Vpu

Summary for 2N28

• Entry DOI: 10.2210/pdb2n28/pdb
• Related: 2N29
• NMR Information: BMRB: 25591
• Descriptor: Protein Vpu (1 entity in total)
• Functional Keywords: alpha helix, viral protein
• Biological source: Human immunodeficiency virus 1 (HIV-1)
• Cellular location: Host membrane ; Single-pass type I membrane protein : P69700
• Total number of polymer chains: 1
• Total formula weight: 9147.64

Authors

Zhang, H.,Lin, E.C.,Tian, Y.,Das, B.B.,Opella, S.J. (deposition date: 2015-05-01, release date: 2015-09-30, Last modification date: 2024-05-01)

Primary citation

Zhang, H.,Lin, E.C.,Das, B.B.,Tian, Y.,Opella, S.J.
Structural determination of virus protein U from HIV-1 by NMR in membrane environments.
Biochim.Biophys.Acta, 1848:3007-3018, 2015

PubMed Abstract: Virus protein U (Vpu) from HIV-1, a small membrane protein composed of a transmembrane helical domain and two α-helices in an amphipathic cytoplasmic domain, down modulates several cellular proteins, including CD4, BST-2/CD317/tetherin, NTB-A, and CCR7. The interactions of Vpu with these proteins interfere with the immune system and enhance the release of newly synthesized virus particles. It is essential to characterize the structure and dynamics of Vpu in order to understand the mechanisms of the protein-protein interactions, and potentially to discover antiviral drugs. In this article, we describe investigations of the cytoplasmic domain of Vpu as well as full-length Vpu by NMR spectroscopy. These studies are complementary to earlier analysis of the transmembrane domain of Vpu. The results suggest that the two helices in the cytoplasmic domain form a U-shape. The length of the inter-helical loop in the cytoplasmic domain and the orientation of the third helix vary with the lipid composition, which demonstrate that the C-terminal helix is relatively flexible, providing accessibility for interaction partners.

PubMed: 26362058
DOI: 10.1016/j.bbamem.2015.09.008

Experimental method

SOLID-STATE NMR