Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR

Quynh, Hoa; Wittlich, Marc; Glück, Julian M.; Möckel, Luis; Willbold, Dieter; Koenig, Bernd W.; Heise, Henrike

doi:10.1515/hsz-2013-0194

Cited by 12 publications

(9 citation statements)

References 59 publications

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“…Marassi et al showed that the TM and Cyto domains of Vpu have distinct orientations with the TM helix approximately parallel to the bilayer normal and Cyto domain perpendicular to the bilayer normal in DPPC/DPPG bilayers aligned on glass plates (24). Similarly, with MAS experiments, the results of Do et al reflect membrane insertion of the TM domain, and the water accessible Cyto domain in POPC bilayers (26). While the three-dimensional structure of Vpu full-length has not been determined previously, the structures of various constructs of the TM domain of Vpu have been well studied in various environments including TFE (27) and detergent micelles (28) by solution NMR, and also in phospholipid bicelles (28), and phospholipid bilayers (29–31) by solid-state NMR.…”

Section: Introductionmentioning

confidence: 83%

“…Solid-state NMR experiments have been applied to Vpu full-length in phospholipid bilayers (24–26). Marassi et al showed that the TM and Cyto domains of Vpu have distinct orientations with the TM helix approximately parallel to the bilayer normal and Cyto domain perpendicular to the bilayer normal in DPPC/DPPG bilayers aligned on glass plates (24).…”

Section: Introductionmentioning

confidence: 99%

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Structural determination of virus protein U from HIV-1 by NMR in membrane environments

Zhang

Lin

Das

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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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.

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Section: Introductionmentioning

confidence: 83%

Section: Introductionmentioning

confidence: 99%

Structural determination of virus protein U from HIV-1 by NMR in membrane environments

Zhang

Lin

Das

et al. 2015

Biochimica et Biophysica Acta (BBA) - Biomembranes

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show abstract

“…The resulting structure showed a mixture of well-defined and highly dynamic regions, which reveals the complicated dynamics of the protein. The effort towards characterizing the full-length Vpu in the native-like bilayer environment can be seen in a recent structural study with MAS solid-state NMR of both Vpu and its interaction partner, CD4, in POPC lipid bilayers (Do Hoa et al, 2013). …”

Section: Examples Of Membrane Proteinsmentioning

confidence: 99%

NMR structures of membrane proteins in phospholipid bilayers

Radoicic

Opella

2014

Quart. Rev. Biophys.

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Membrane proteins have always presented technical challenges for structural studies because of their requirement for a lipid environment. Multiple approaches exist including X-ray crystallography and electron microscopy that can give significant insights into their structure and function. However, nuclear magnetic resonance (NMR) is unique in that it offers the possibility of determining the structures of unmodified membrane proteins in their native environment of phospholipid bilayers under physiological conditions. Furthermore, NMR enables the characterization of the structure and dynamics of backbone and side chain sites of the proteins alone and in complexes with both small molecules and other biopolymers. The learning curve has been steep for the field as most initial studies were performed under non-native environments using modified proteins until ultimately progress in both techniques and instrumentation led to the possibility of examining unmodified membrane proteins in phospholipid bilayers under physiological conditions. This review aims to provide an overview of the development and application of NMR to membrane proteins. It highlights some of the most significant structural milestones that have been reached by NMR spectroscopy of membrane proteins; especially those accomplished with the proteins in phospholipid bilayer environments where they function.

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“…In addition, site-specific information about solvent exposure was provided by H-D exchange experiments. Later, Do et al characterized full-length Vpu in POPC bilayers using MAS NMR [199]. Partial resonance assignments for 13 C were obtained by examining uniformly labeled protein, supporting the α-helical conformation in the TM domain.…”

Section: Structure and Dynamics Of Viral Systems With Mas Nmrmentioning

confidence: 99%

Magic angle spinning NMR of viruses

Quinn

Suiter

et al. 2015

Progress in Nuclear Magnetic Resonance Spectroscopy

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Viruses, relatively simple pathogens, are able to replicate in many living organisms and to adapt to various environments. Conventional atomic-resolution structural biology techniques, X-ray crystallography and solution NMR spectroscopy provided abundant information on the structures of individual proteins and nucleic acids comprising viruses; however, viral assemblies are not amenable to analysis by these techniques because of their large size, insolubility, and inherent lack of long-range order. In this article, we review the recent advances in magic angle spinning NMR spectroscopy that enabled atomic-resolution analysis of structure and dynamics of large viral systems and give examples of several exciting case studies.

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Full-length Vpu and human CD4(372–433) in phospholipid bilayers as seen by magic angle spinning NMR

Cited by 12 publications

References 59 publications

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

NMR structures of membrane proteins in phospholipid bilayers

Magic angle spinning NMR of viruses

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