ArticleThe Journal of biological chemistry2014
Human cytochrome P450 17A1 conformational selection: modulation by ligand and cytochrome b5.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 71 citations in OpenAlex.
- On the interface of fatty acid metabolism: A crosstalk between fatty acid ω-hydroxylase CYP4F11 and fatty acid desaturase 2 in non-small cell lung cancer.Drug metabolism and disposition: the biological fate of chemicals · 2026Article
- Identification of Isovitexin as a novel CYP17A1 inhibitor through virtual screening and evaluation of its anti-cancer effects in MCF-7 breast cancer cells.Medical oncology (Northwood, London, England) · 2025Article
- Steroidogenic cytochrome P450 enzymes as drug target.Toxicological research · 2024Review
- Tracking protein-protein interactions by NMR: conformational selection in human steroidogenic cytochrome P450 CYP17A1 induced by cytochromePhysical chemistry chemical physics : PCCP · 2024Article
- Differential Effects of Clotrimazole on X-Ray Crystal Structures of Human Cytochromes P450 3A5 and 3A4.Drug metabolism and disposition: the biological fate of chemicals · 2023Article
- Direct interaction between the transmembrane helices stabilize cytochrome P450 2B4 and cytochrome b5 redox complex.Biophysical chemistry · 2023Article
- Selective steroidogenic cytochrome P450 haem iron ligation by steroid-derived isonitriles.Communications chemistry · 2023Article
- Allosteric modulation of cytochrome P450 enzymes by the NADPH cytochrome P450 reductase FMN-containing domain.The Journal of biological chemistry · 2023Article
- Non-steroidal CYP17A1 Inhibitors: Discovery and Assessment.Journal of medicinal chemistry · 2023Review
- Conformational heterogeneity suggests multiple substrate binding modes in CYP106A2.Journal of inorganic biochemistry · 2023Article
- Hydroxylation and lyase reactions of steroids catalyzed by mouse cytochrome P450 17A1 (Cyp17a1).Journal of inorganic biochemistry · 2023Article
- Four Decades of Cytochrome P450 2B Research: From Protein Adducts to Protein Structures and Beyond.Drug metabolism and disposition: the biological fate of chemicals · 2023Review
- Steroid 17α-hydroxylase/17, 20-lyase (cytochrome P450 17A1).Methods in enzymology · 2023Article
- Redox partner adrenodoxin alters cytochrome P450 11B1 ligand binding and inhibition.Journal of inorganic biochemistry · 2022Article
- Binding of cytochrome P450 27C1, a retinoid desaturase, to its accessory protein adrenodoxin.Archives of biochemistry and biophysics · 2021Article
- Progesterone receptor membrane component 1 (PGRMC1) binds and stabilizes cytochromes P450 through a heme-independent mechanism.The Journal of biological chemistry · 2021Article
- A dynamic understanding of cytochrome P450 structure and function through solution NMR.Current opinion in biotechnology · 2021Review
- Steroidogenic cytochrome P450 17A1 structure and function.Molecular and cellular endocrinology · 2021Review
- Substrate-Specific Allosteric Effects on the Enhancement of CYP17A1 Lyase Efficiency by CytochromeJournal of the American Chemical Society · 2021Article
- An electron transfer competent structural ensemble of membrane-bound cytochrome P450 1A1 and cytochrome P450 oxidoreductase.Communications biology · 2021Article
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4 authors at 1 institution in 1 country.
Funding
Abstract
Crystallographic studies of different membrane cytochrome P450 enzymes have provided examples of distinct structural conformations, suggesting protein flexibility. It has been speculated that conformational selection is an integral component of substrate recognition and access, but direct evidence of such substate interconversion has thus far remained elusive. In the current study, solution NMR revealed multiple and exchanging backbone conformations for certain structural features of the human steroidogenic cytochrome P450 17A1 (CYP17A1). This bifunctional enzyme is responsible for pregnenolone C17 hydroxylation, followed by a 17,20-lyase reaction to produce dehydroepiandrosterone, the key intermediate in human synthesis of androgen and estrogen sex steroids. The distribution of CYP17A1 conformational states was influenced by temperature, binding of these two substrates, and binding of the soluble domain of cytochrome b5 (b5). Notably, titration of b5 to CYP17A1·pregnenolone induced a set of conformational states closely resembling those of CYP17A1·17α-hydroxypregnenolone without b5, providing structural evidence consistent with the reported ability of b5 to selectively enhance 17,20-lyase activity. Solution NMR thus revealed a set of conformations likely to modulate human steroidogenesis by CYP17A1, demonstrating that this approach has the potential to make similar contributions to understanding the functions of other membrane P450 enzymes involved in drug metabolism and disease states.
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