Pair your accounts.

Export articles to Mendeley

Get article recommendations from ACS based on references in your Mendeley library.

Pair your accounts.

Export articles to Mendeley

Get article recommendations from ACS based on references in your Mendeley library.

You’ve supercharged your research process with ACS and Mendeley!

STEP 1:
Click to create an ACS ID

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

Please note: If you switch to a different device, you may be asked to login again with only your ACS ID.

MENDELEY PAIRING EXPIRED
Your Mendeley pairing has expired. Please reconnect
ACS Publications. Most Trusted. Most Cited. Most Read
Homology Models and Molecular Modeling of Human Retinoic Acid Metabolizing Enzymes Cytochrome P450 26A1 (CYP26A1) and P450 26B1 (CYP26B1)
My Activity
CONTENT TYPES

Figure 1Loading Img
    Article

    Homology Models and Molecular Modeling of Human Retinoic Acid Metabolizing Enzymes Cytochrome P450 26A1 (CYP26A1) and P450 26B1 (CYP26B1)
    Click to copy article linkArticle link copied!

    View Author Information
    Department of Natural Sciences and Örebro Life Science Center, Modeling and Simulation Research Center, and Department of Clinical Medicine, Örebro University, 70182 Örebro, Sweden
    * Corresponding author e-mail: [email protected]
    †Department of Natural Sciences and Örebro Life Science Center, Örebro University.
    ‡Modeling and Simulation Research Center, Örebro University.
    §Department of Clinical Medicine and Örebro Life Science Center, Örebro University.
    Other Access Options

    Journal of Chemical Theory and Computation

    Cite this: J. Chem. Theory Comput. 2008, 4, 6, 1021–1027
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ct800033x
    Published May 2, 2008
    Copyright © 2008 American Chemical Society

    Abstract

    Click to copy section linkSection link copied!

    Homology models of cytochrome P450 26A1 and cytochrome P450 26B1 were constructed using the crystal structures of human, CYP2C8, CYP2C9, and CYP3A4 as templates for the model building. The homology models generated were investigated for their docking capacities against the natural substrate all-trans-retinoic acid (atRA), five different tetralone-derived retinoic acid metabolizing blocking agents (RAMBAs), and R115866. Interaction energies (IE) and linear interaction energies (LIE) were calculated for all inhibitors in both homology models after molecular dynamics (MD) simulation of the enzyme−ligand complexes. The results revealed that the homologues had the capacity to distinguish between strong and weak inhibitors. Important residues in the active site were identified from the CYP26A1/B1−atRA complexes. Residues involved in hydrophobic interactions with atRA were Pro113, Phe222, Phe299, Val370, Pro371, and Phe374 in CYP26A1 and Leu88, Pro118, Phe222, Phe295, Ile368, and Tyr272 in CYP26B1. Hydrogen bonding interactions were observed between the atRA carboxylate group and Arg 90 in CYP26A1 and with Arg76, Arg95, and Ser369 in CYP26B1.

    Copyright © 2008 American Chemical Society

    Read this article

    To access this article, please review the available access options below.

    Get instant access

    Purchase Access

    Read this article for 48 hours. Check out below using your ACS ID or as a guest.

    Recommended

    Access through Your Institution

    You may have access to this article through your institution.

    Your institution does not have access to this content. Add or change your institution or let them know you’d like them to include access.

    Cited By

    Click to copy section linkSection link copied!

    This article is cited by 14 publications.

    1. Patricia Saenz-Méndez, Ali Ateia Elmabsout, Helena Sävenstrand, Mohamed Khalid Alhaj Awadalla, Åke Strid, Allan Sirsjö, and Leif A. Eriksson . Homology Models of Human All-Trans Retinoic Acid Metabolizing Enzymes CYP26B1 and CYP26B1 Spliced Variant. Journal of Chemical Information and Modeling 2012, 52 (10) , 2631-2637. https://doi.org/10.1021/ci300264u
    2. Johannes Kirchmair, Mark J. Williamson, Jonathan D. Tyzack, Lu Tan, Peter J. Bond, Andreas Bender, and Robert C. Glen . Computational Prediction of Metabolism: Sites, Products, SAR, P450 Enzyme Dynamics, and Mechanisms. Journal of Chemical Information and Modeling 2012, 52 (3) , 617-648. https://doi.org/10.1021/ci200542m
    3. Nina Isoherranen, Guo Zhong. Biochemical and physiological importance of the CYP26 retinoic acid hydroxylases. Pharmacology & Therapeutics 2019, 204 , 107400. https://doi.org/10.1016/j.pharmthera.2019.107400
    4. Guo Zhong, David Ortiz, Alex Zelter, Abhinav Nath, Nina Isoherranen. CYP26C1 Is a Hydroxylase of Multiple Active Retinoids and Interacts with Cellular Retinoic Acid Binding Proteins. Molecular Pharmacology 2018, 93 (5) , 489-503. https://doi.org/10.1124/mol.117.111039
    5. Robert S. Foti, Philippe Diaz, Dominique Douguet. Comparison of the ligand binding site of CYP2C8 with CYP26A1 and CYP26B1: a structural basis for the identification of new inhibitors of the retinoic acid hydroxylases. Journal of Enzyme Inhibition and Medicinal Chemistry 2016, 31 (sup2) , 148-161. https://doi.org/10.1080/14756366.2016.1193734
    6. R. S. Foti, N. Isoherranen, A. Zelter, L. J. Dickmann, B. R. Buttrick, P. Diaz, D. Douguet. Identification of Tazarotenic Acid as the First Xenobiotic Substrate of Human Retinoic Acid Hydroxylase CYP26A1 and CYP26B1. Journal of Pharmacology and Experimental Therapeutics 2016, 357 (2) , 281-292. https://doi.org/10.1124/jpet.116.232637
    7. Mohamed Awadalla, Thamir Alshammari, Leif Eriksson, Patricia Saenz-Méndez. Improved Homology Model of the Human all-trans Retinoic Acid Metabolizing Enzyme CYP26A1. Molecules 2016, 21 (3) , 351. https://doi.org/10.3390/molecules21030351
    8. Sébastien P. Blais, Jack A. Kornblatt, Xavier Barbeau, Guillaume Bonnaure, Patrick Lagüe, Robert Chênevert, Jacques Lapointe, . tRNAGlu Increases the Affinity of Glutamyl-tRNA Synthetase for Its Inhibitor Glutamyl-Sulfamoyl-Adenosine, an Analogue of the Aminoacylation Reaction Intermediate Glutamyl-AMP: Mechanistic and Evolutionary Implications. PLOS ONE 2015, 10 (4) , e0121043. https://doi.org/10.1371/journal.pone.0121043
    9. Mark J. Williamson. Computational Free Energy Methods for Ascertaining Ligand Interaction with Metabolizing Enzymes. 2014, 179-198. https://doi.org/10.1002/9783527673261.ch07
    10. Stéphanie Dallaire-Dufresne, Xavier Barbeau, Darren Sarty, Katherine H. Tanaka, Alix M. Denoncourt, Patrick Lagüe, Michael E. Reith, Steve J. Charette. Aeromonas salmonicida Ati2 is an effector protein of the type three secretion system. Microbiology 2013, 159 (Pt_9) , 1937-1945. https://doi.org/10.1099/mic.0.067959-0
    11. Jakob A. Shimshoni, Arthur G. Roberts, Michele Scian, Ariel R. Topletz, Sean A. Blankert, James R. Halpert, Wendel L. Nelson, Nina Isoherranen. Stereoselective Formation and Metabolism of 4-Hydroxy-Retinoic Acid Enantiomers by Cytochrome P450 Enzymes. Journal of Biological Chemistry 2012, 287 (50) , 42223-42232. https://doi.org/10.1074/jbc.M112.404475
    12. Ariel R. Topletz, Jayne E. Thatcher, Alex Zelter, Justin D. Lutz, Suzanne Tay, Wendel L. Nelson, Nina Isoherranen. Comparison of the function and expression of CYP26A1 and CYP26B1, the two retinoic acid hydroxylases. Biochemical Pharmacology 2012, 83 (1) , 149-163. https://doi.org/10.1016/j.bcp.2011.10.007
    13. Jayne E. Thatcher, Brian Buttrick, Scott A. Shaffer, Jakob A. Shimshoni, David R. Goodlett, Wendel L. Nelson, Nina Isoherranen. Substrate Specificity and Ligand Interactions of CYP26A1, the Human Liver Retinoic Acid Hydroxylase. Molecular Pharmacology 2011, 80 (2) , 228-239. https://doi.org/10.1124/mol.111.072413
    14. Bing Wu, Jie Sun, Shu-Pei Cheng, Ji-Dong Gu, Ai-Min Li, Xu-Xiang Zhang. Comparative analysis of binding affinities between styrene and mammalian CYP2E1 by bioinformatics approaches. Ecotoxicology 2011, 20 (5) , 1041-1046. https://doi.org/10.1007/s10646-011-0643-z

    Journal of Chemical Theory and Computation

    Cite this: J. Chem. Theory Comput. 2008, 4, 6, 1021–1027
    Click to copy citationCitation copied!
    https://doi.org/10.1021/ct800033x
    Published May 2, 2008
    Copyright © 2008 American Chemical Society

    Article Views

    613

    Altmetric

    -

    Citations

    Learn about these metrics

    Article Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.

    Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.

    The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated.