β<sub>2</sub>‐Adrenergic Receptor Solutions for Structural Biology Analyzed with Microscale NMR Diffusion Measurements

Horst, Reto; Stańczak, Paweł; Stevens, Raymond C.; Wüthrich, Kurt

doi:10.1002/ange.201205474

Angewandte Chemie

2012

DOI: 10.1002/ange.201205474

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β₂‐Adrenergic Receptor Solutions for Structural Biology Analyzed with Microscale NMR Diffusion Measurements

Reto Horst

Paweł Stańczak

Raymond C. Stevens

et al.

Abstract: Mikrospulen‐NMR‐Messungen wurden durchgeführt, um die Zusammensetzung von detergenshaltigen β2‐Adrenozeptor‐Lösungen (β2AR) zu bestimmen und die hydrodynamischen Eigenschaften der β2AR‐Detergensmicellen (siehe Bild) zu untersuchen. Es werden Standards zur reproduzierbaren Herstellung von Lösungen G‐Protein‐gekoppelter Rezeptoren für Kristallisationsversuche und Flüssig‐NMR‐Untersuchungen etabliert.

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Cited by 2 publications

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References 23 publications

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“…extended, the MWC model, emphasizing in particular "population shifts" of discrete conformations within an energy landscape formalism (see [10][11][12][13][14] ; Figure 1B, bottom).…”

mentioning

confidence: 99%

Allosteric Modulation as a Unifying Mechanism for Receptor Function and Regulation

Changeux

Christopoulos

2016

Cell

261

161

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Four major receptor families enable cells to respond to chemical and physical signals from their proximal environment. The ligand-and voltage-gated ion channels, G-protein-coupled receptors, nuclear hormone receptors and receptor tyrosine kinases are all allosteric proteins that carry multiple, spatially distinct, yet conformationally linked ligand-binding sites. Recent studies point to common mechanisms governing the allosteric transitions of these receptors, including the impact of oligomerization, pre-existing and functionally distinct conformational ensembles, intrinsically disordered regions, and the occurrence of allosteric modulatory sites. Importantly, synthetic allosteric modulators are being discovered for these receptors, providing an enriched, yet challenging, landscape for novel therapeutics.

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“…extended, the MWC model, emphasizing in particular "population shifts" of discrete conformations within an energy landscape formalism (see [10][11][12][13][14] ; Figure 1B, bottom).…”

mentioning

confidence: 99%

Allosteric Modulation as a Unifying Mechanism for Receptor Function and Regulation

Changeux

Christopoulos

2016

Cell

261

161

View full text Add to dashboard Cite

show abstract

Solution‐NMR Characterization of Outer‐Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles

2014

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X-ray crystallography and solution NMR of detergent-reconstituted OmpA (outer membrane protein A from E. coli) had shown that this protein forms an 8-stranded transmembrane β-barrel, but only limited information was obtained for the extracellular loops. In NMR studies of OmpA in two different detergent micelles, “NMR-invisible” amino acid residues in-between the extracellular loops and the β-barrel prevented complete structural characterization. Here, we show that this NMR-invisible ring around the β-barrel of OmpA is present also in lipid bilayer nanodiscs and in mixed micelles with a third detergent, suggesting that the implicated rate processes have a functional role rather than representing an artifact of the protein reconstitution. In addition to sequence-specific NMR assignments for OmpA in the nanodiscs, the present results are based on a protocol of micro-coil TROSY- and CRINEPT-type NMR diffusion measurements for studying the hydrodynamic properties and the foldedness of [2H,15N]-labeled membrane proteins in nanodiscs, which can be applied under closely similar conditions to those used for NMR structure determinations or crystallization trials.

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β₂‐Adrenergic Receptor Solutions for Structural Biology Analyzed with Microscale NMR Diffusion Measurements

Cited by 2 publications

References 23 publications

Allosteric Modulation as a Unifying Mechanism for Receptor Function and Regulation

Allosteric Modulation as a Unifying Mechanism for Receptor Function and Regulation

Solution‐NMR Characterization of Outer‐Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles

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β2‐Adrenergic Receptor Solutions for Structural Biology Analyzed with Microscale NMR Diffusion Measurements

Cited by 2 publications

References 23 publications

Allosteric Modulation as a Unifying Mechanism for Receptor Function and Regulation

Allosteric Modulation as a Unifying Mechanism for Receptor Function and Regulation

Solution‐NMR Characterization of Outer‐Membrane Protein A from E. coli in Lipid Bilayer Nanodiscs and Detergent Micelles

Contact Info

Product

Resources

About

β₂‐Adrenergic Receptor Solutions for Structural Biology Analyzed with Microscale NMR Diffusion Measurements