Evidence map›Paper›PMID 32464592›Full record

ArticleJournal of inorganic biochemistry2020

Conformational selection is present in ligand binding to cytochrome P450 19A1 lipoprotein nanodiscs.

Francisco Zárate-Pérez, John C Hackett

Abstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Selectivity of osilodrostat as an inhibitor of human steroidogenic cytochromes P450.The Journal of steroid biochemistry and molecular biology · 2023
    Article
  9. Article
  10. Article
  11. Nanodiscs: A toolkit for membrane protein science.Protein science : a publication of the Protein Society · 2021
    Review
  12. Mechanisms of ligand binding.Biophysics reviews · 2020
    Review
  13. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors.

Francisco Zárate-PérezDepartment of Physiology and Biophysics and The Massey Cancer Center, Virginia Commonwealth University School of Medicine, Richmond, VA 23298, United States of America.
John C HackettDepartment of Physiology and Biophysics and The Massey Cancer Center, Virginia Commonwealth University School of Medicine, Richmond, VA 23298, United States of America. Electronic address: john.hackett@vcuhealth.org.

Funding

Computational and Vibrational Probes of CYP3A4 Solution DynamicsR01GM114168 · NIGMS · VIRGINIA COMMONWEALTH UNIVERSITY · PI HACKETT, JOHN C · 2015 to 2018
$1.3M
NIGMS NIH HHS R01 GM114168
6 · The paper itself

Abstract

Cytochromes P450 (CYPs) display remarkable plasticity in their ability to bind substrates and catalyze a broad array of chemical reactions. Herein we evaluate binding of androstenedione, testosterone, and 7-hydroxyflavone to CYP19A1, also known as aromatase, in phospholipid nanodiscs by stopped-flow UV-vis spectroscopy. Exponential fitting of the kinetic traces supports the possibility of a multi-step binding mechanism. Subsequent global fitting of the data to the solutions of the coupled differential equations describing the fundamental mechanisms of induced fit and conformational selection, consistently support presence of the latter. To our knowledge, this is the first discrimination of conformational selection from induced fit for a mono-disperse CYP in a native-like membrane environment. In addition, 7-hydroxyflavone binds to CYP19A1 nanodiscs with comparable affinity to the substrates and induces an unusual spectral response likely attributable to hydrogen bonding to, rather than displacement of the heme-coordinated water molecule.

Indexed as

AndrostenedioneAromataseCatalysisFlavonoidsHumansKineticsLigandsLipoproteinsModels, TheoreticalNanoparticlesProtein BindingProtein ConformationSpectrum AnalysisTestosterone7-hydroxyflavoneAndrostenedioneAromataseCYP19A1 protein, humanFlavonoidsLigandsLipoproteinsTestosteroneAromataseConformational selectionCYP19A1Cytochrome P450Induced fitStopped-flow UV–vis spectroscopy

Identifiers

PMID32464592
PMCPMC7483944

What OpenQuestion holds

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Read underepoch 390

Registered trials

None linked

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.