Cited by 707Pharmacogenetics and Drug MetabolismMetal-Catalyzed Oxygenation MechanismsEnzyme Structure and Function

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Mammalian Microsomal Cytochrome P450 Monooxygenase

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Williams, Pamela A., Cosme, Jose, Sridhar, Vandana, Johnson, Eric F., McRee, Duncan E.·2000·Molecular Cell

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Abstract

Microsomal cytochrome P450s participate in xenobiotic detoxification, procarcinogen activation, and steroid hormone synthesis. The first structure of a mammalian microsomal P450 suggests that the association of P450s with the endoplasmic reticulum involves a hydrophobic surface of the protein formed by noncontiguous portions of the polypeptide chain. This interaction places the entrance of the putative substrate access channel in or near the membrane and orients the face of the protein proximal to the heme cofactor perpendicular to the plane of the membrane for interaction with the P450 reductase. This structure offers a template for modeling other mammalian P450s and should aid drug discovery and the prediction of drug-drug interactions.

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[20] Processing of X-ray diffraction data collected in oscillation mode
Otwinowski, Z., & Minor, W. (1997) · Methods in Enzymology · doi:10.1016/s0076-6879(97)76066-x · Cited by 33,475
The CCP4 suite: programs for protein crystallography
Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,317
Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
Brünger, A. T., Adams, P. D., Clore, G. M., DeLano, W. L., Gros, P., Grosse‐Kunstleve, R. W., Jiang, J., Kuszewski, J. J., Nilges, M., Pannu, N., et al. (1998) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444998003254 · Cited by 15,723
Free R value: a novel statistical quantity for assessing the accuracy of crystal structures
Brünger, A. T. (1992) · Nature · doi:10.1038/355472a0 · Cited by 3,877
Classical Electrostatics in Biology and Chemistry
Honig, B. H., & Nicholls, A. O. (1995) · Science · doi:10.1126/science.7761829 · Cited by 2,891
XtalView/Xfit—A Versatile Program for Manipulating Atomic Coordinates and Electron Density
McRee, D. E. (1999) · Journal of Structural Biology · doi:10.1006/jsbi.1999.4094 · Cited by 2,096
Self-citation
Improved Fourier coefficients for maps using phases from partial structures with errors
Read, R. J. (1986) · Acta Crystallographica Section A Foundations of Crystallography · doi:10.1107/s0108767386099622 · Cited by 1,870
IDENTIFYING NONPOLAR TRANSBILAYER HELICES IN AMINO ACID SEQUENCES OF MEMBRANE PROTEINS
Engelman, D. M., Steitz, T. A., & Goldman, A. (1986) · Annual Review of Biophysics and Biophysical Chemistry · doi:10.1146/annurev.bb.15.060186.001541 · Cited by 1,508
HIGH-RESOLUTION CRYSTAL STRUCTURE OF CYTOCHROME P450-CAM
Poulos, T. L., Finzel, B. C., & Howard, A. J. (1987) · Journal of Molecular Biology · doi:10.1016/0022-2836(87)90190-2 · Cited by 1,419
Substrate recognition sites in cytochrome P450 family 2 (CYP2) proteins inferred from comparative analyses of amino acid and coding nucleotide sequences.
Gotoh, O. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48462-1 · Cited by 1,204

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Authors: Williams, P. A., Cosme, J., Sridhar, V., Johnson, E. F., & McRee, D. E.
Affiliations: Scripps Research Institute (US)
Corresponding author: McRee, Duncan E.
ORCID: Williams, Pamela A.
Johnson, Eric F.
McRee, Duncan E.
Venue: Molecular Cell
Publisher: Elsevier BV
Published: 2000-01
Volume: 5
Issue: 1
Pages: 121-131
ISSN: 1097-2765 (ISSN-L)
DOI: 10.1016/s1097-2765(00)80408-6
OpenAlex: W2051639214
Cited by: 696
References: 52
Citations by year: 2026: 4 · 2025: 5 · 2024: 10 · 2023: 5 · 2022: 8 · 2021: 7 · 2020: 19 · 2019: 15 · 2018: 18 · 2017: 18 · 2016: 21 · 2015: 13 · 2014: 18 · 2013: 20 · 2012: 11
FWCI: 53.02
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4946 d)
Locations: Molecular Cell (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (5p01gm048495-08)
National Institute of General Medical Sciences (R01GM031001, GM-31001, GM-48495)
Topics: Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Pharmacology › Pharmacogenetics and Drug Metabolism
Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords: cytochrome P450, endoplasmic reticulum, protein structure, NADPH-cytochrome P450 reductase, xenobiotic detoxification, procarcinogen activation, steroidogenesis, drug-drug interactions, drug discovery
MeSH terms: Cytochrome P450 Family 2, Amino Acid Sequence, Animals, Binding Sites, Cytochrome P-450 Enzyme System, Endoplasmic Reticulum, Heme, Mammals, Microsomes, Models, Molecular, Molecular Sequence Data, Steroid 21-Hydroxylase, Protein Structure, Secondary, Crystallography, X-Ray

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Mammalian Microsomal Cytochrome P450 Monooxygenase

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