Related ArticlesStructural determination of Virus protein U from HIV-1 by NMR in membrane environments.
Biochim Biophys Acta. 2015 Sep 8;
Authors: Zhang H, Lin EC, Das BB, Tian Y, Opella SJ
Abstract
Virus protein U (Vpu) from HIV-1, a small membrane protein composed of a transmembrane helical domain and two ?-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.
PMID: 26362058 [PubMed - as supplied by publisher]
Structural determination of Virus protein U from HIV-1 by NMR in membrane environments
Structural determination of Virus protein U from HIV-1 by NMR in membrane environments
Publication date: Available online 8 September 2015
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes</br>
Author(s): Hua Zhang, Eugene C. Lin, Bibhuti B. Das, Ye Tian, Stanley J. Opella</br>
Virus protein U (Vpu) from HIV-1, a small membrane protein composed of a transmembrane helical domain and two ?-helices in an amphipathic cytoplasmic domain, down modulates several cellular proteins, including CD4, BST-2/CD317/tetherin, NTB-A, and CCR7. The interactions of...
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09-08-2015 11:26 PM
[NMR paper] Membrane topology of NS2B of dengue virus revealed by NMR spectroscopy.
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Biochim Biophys Acta. 2015 Jun 11;
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Non-structural (NS) proteins of dengue virus (DENV) are important for viral replication. There are four membrane proteins that are coded by viral genome. NS2B was shown to be one of the membrane proteins and its main function was confirmed to regulate viral protease activity. Its...
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Abstract
A wide variety of membrane proteins induce membrane curvature for function, thus it is important to develop...
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[NMR paper] Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy.
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Abstract
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Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments.
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Biochim Biophys Acta. 2011 Jul 23;
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Fragments of integral membrane proteins have been used to study the physical chemical properties of regions of transporters and receptors. Ste2p(G31-T110) is an 80-residue polypeptide which contains a...
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A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.
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Eur Biophys J. 2011 Apr;40(4):447-62
Authors: Toke O, Bánóczi Z, Király P, Heinzmann R, Bürck J, Ulrich AS, Hudecz F
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The LAH4 family of histidine-rich peptides exhibits potent antimicrobial and DNA transfection activities, both of which require interactions...
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Authors: Lin TH, Chia CM, Hsiao JC, Chang W, Ku CC, Hung SC, Tzou DL
This study presents the molecular structure of the extracellular domain of vaccinia virus envelope protein, A27L, determined by NMR and CD spectroscopy. A recombinant protein, eA27L-aa,...
Structural determination of Virus protein U from HIV-1 by NMR in membrane environments.
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