ArticleBiochemistry2007
Magic-angle spinning solid-state NMR spectroscopy of nanodisc-embedded human CYP3A4.
Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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The trial behind it
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Who cites it
46 citing papers in PubMed, 104 citations in OpenAlex.
- Oversized nanodiscs for combined structural and functional investigation of multicomponent membrane protein systems.Scientific reports · 2025Article
- Nanodisc Technology: Direction toward Physicochemical Characterization of Chemosensory Membrane Proteins in Food Flavor Research.Journal of agricultural and food chemistry · 2024Review
- Nanodisc Reconstitution and Characterization of Amyloid-β Precursor Protein C99.Analytical chemistry · 2024Article
- Nanodisc reconstitution and characterization of amyloid-β precursor protein C99.bioRxiv : the preprint server for biology · 2024Article
- Detergent-Free Isolation of Membrane Proteins and Strategies to Study Them in a Near-Native Membrane Environment.Biomolecules · 2022Review
- Lipid Membrane Mimetics in Functional and Structural Studies of Integral Membrane Proteins.Membranes · 2021Review
- Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021Review
- Crystallization of ApoA1 and ApoE4 nanolipoprotein particles and initial XFEL-based structural studies.Crystals · 2020Article
- Nanodiscs: A Controlled Bilayer Surface for the Study of Membrane Proteins.Annual review of biophysics · 2018Article
- Assembly of phospholipid nanodiscs of controlled size for structural studies of membrane proteins by NMR.Nature protocols · 2018Article
- Microfluidic platform for efficient Nanodisc assembly, membrane protein incorporation, and purification.Lab on a chip · 2017Article
- Transmembrane Interactions of Full-length Mammalian Bitopic Cytochrome-P450-Cytochrome-bScientific reports · 2017Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- Proton-Detected Solid-State NMR Spectroscopy of a Zinc Diffusion Facilitator Protein in Native Nanodiscs.Angewandte Chemie (International ed. in English) · 2017Article
- Advances in the Understanding of Protein-Protein Interactions in Drug Metabolizing Enzymes through the Use of Biophysical Techniques.Frontiers in pharmacology · 2017Review
- Nanodiscs for structural and functional studies of membrane proteins.Nature structural & molecular biology · 2016Review
- Solid-state NMR of the Yersinia pestis outer membrane protein Ail in lipid bilayer nanodiscs sedimented by ultracentrifugation.Journal of biomolecular NMR · 2015Article
- Membrane protein structure from rotational diffusion.Biochimica et biophysica acta · 2015Review
- Current Approaches for Investigating and Predicting Cytochrome P450 3A4-Ligand Interactions.Advances in experimental medicine and biology · 2015Review
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cytochrome P450 (CYP) 3A4 contributes to the metabolism of approximately 50% of commercial drugs by oxidizing a large number of structurally diverse substrates. Like other endoplasmic reticulum-localized P450s, CYP3A4 contains a membrane-anchoring N-terminal helix and a significant number of hydrophobic domains, important for the interaction between CYP3A4 and the membrane. Although the membrane affects specificity of CYP3A4 ligand binding, the structural details of the interaction have not been revealed so far because X-ray crystallography studies are available only for the soluble domain of CYP3A4. Here we report sample preparation and initial magic-angle spinning (MAS) solid-state NMR (SSNMR) of CYP3A4 (Delta3-12) embedded in a nanoscale membrane bilayer, or Nanodisc. The growth protocol yields approximately 2.5 mg of the enzymatically active, uniformly 13C,15N-enriched CYP3A4 from 1 L of growth medium. Polyethylene glycol 3350-precipitated CYP3A4 in Nanodiscs yields spectra of high resolution and sensitivity, consistent with a folded, homogeneous protein. CYP3A4 in Nanodiscs remains enzymatically active throughout the precipitation protocol as monitored by bromocriptine binding. The 13C line widths measured from 13C-13C 2D chemical shift correlation spectra are approximately 0.5 ppm. The secondary structure distribution within several amino acid types determined from 13C chemical shifts is consistent with the ligand-free X-ray structures. These results demonstrate that MAS SSNMR can be performed on Nanodisc-embedded membrane proteins in a folded, active state. The combination of SSNMR and Nanodisc methodologies opens up new possibilities for obtaining structural information on CYP3A4 and other integral membrane proteins with full retention of functionality.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.