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Covalently circularized nanodiscs for studying membrane proteins and viral entry

by Huser, Sonja , Hagn, Franz , Nasr, Mahmoud L , Baptista, Diego , Strauss, Mike , Grigoriu, Simina , Wagner, Gerhard , Sun, Zhen-Yu J , Plückthun, Andreas , Hogle, James M , Walz, Thomas

in 101/28 / 631/1647/2230/2233 / 631/1647/2258/878 / 631/45/612/1237 / 631/92/96 / 82/83 / Analysis / Bioengineering / Bioinformatics / Biological Microscopy / Biological Techniques / Biomedical Engineering/Biotechnology / brief-communication / Humans / Life Sciences / Lipid Bilayers - chemistry / Lipid Bilayers - metabolism / Membrane proteins / Membranes / Models, Molecular / Nanoparticles / Nanostructures - chemistry / NMR / Nuclear magnetic resonance / Nuclear magnetic resonance spectroscopy / Nuclear Magnetic Resonance, Biomolecular / Poliomyelitis - metabolism / Poliomyelitis - virology / Poliovirus - physiology / Protein engineering / Proteins / Proteomics / Receptors, Neurotensin - metabolism / Virus Internalization / Voltage-Dependent Anion Channel 1 - metabolism

2017

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Covalently circularized nanodiscs for studying membrane proteins and viral entry

by Huser, Sonja , Hagn, Franz , Nasr, Mahmoud L , Baptista, Diego , Strauss, Mike , Grigoriu, Simina , Wagner, Gerhard , Sun, Zhen-Yu J , Plückthun, Andreas , Hogle, James M , Walz, Thomas

2017

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Covalently circularized nanodiscs for studying membrane proteins and viral entry

by Huser, Sonja , Hagn, Franz , Nasr, Mahmoud L , Baptista, Diego , Strauss, Mike , Grigoriu, Simina , Wagner, Gerhard , Sun, Zhen-Yu J , Plückthun, Andreas , Hogle, James M , Walz, Thomas

2017

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Journal Article

Covalently circularized nanodiscs for studying membrane proteins and viral entry

Huser, Sonja,

Hagn, Franz,

Nasr, Mahmoud L,

Baptista, Diego,

Strauss, Mike,

Grigoriu, Simina,

Wagner, Gerhard,

Sun, Zhen-Yu J,

Plückthun, Andreas,

Hogle, James M,

Walz, Thomas

2017

Overview

Membrane proteins can be stabilized in a native-like setting using lipid-bilayer-based nanodiscs encircled by a membrane scaffold protein. Covalently circularized nanodiscs now offer enhanced stability and control over nanodisc diameter size, improving the quality of structural data. We engineered covalently circularized nanodiscs (cNDs) which, compared with standard nanodiscs, exhibit enhanced stability, defined diameter sizes and tunable shapes. Reconstitution into cNDs enhanced the quality of nuclear magnetic resonance spectra for both VDAC-1, a β-barrel membrane protein, and the G-protein-coupled receptor NTR1, an α-helical membrane protein. In addition, we used cNDs to visualize how simple, nonenveloped viruses translocate their genomes across membranes to initiate infection.

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Publisher

Nature Publishing Group US,Nature Publishing Group

Subject

/ 82/83