Next Article in Journal
Self-Assembled Modified Soy Protein/Dextran Nanogel Induced by Ultrasonication as a Delivery Vehicle for Riboflavin
Next Article in Special Issue
Calculation of Relative Binding Free Energy in the Water-Filled Active Site of Oligopeptide-Binding Protein A
Previous Article in Journal
Solid-Phase Synthesis of Amine/Carboxyl Substituted Prolines and Proline Homologues: Scope and Limitations
Previous Article in Special Issue
Exploration of Scaffolds from Natural Products with Antiplasmodial Activities, Currently Registered Antimalarial Drugs and Public Malarial Screen Data
Article Menu
Issue 3 (March) cover image

Export Article

Open AccessArticle
Molecules 2016, 21(3), 351; doi:10.3390/molecules21030351

Improved Homology Model of the Human all-trans Retinoic Acid Metabolizing Enzyme CYP26A1

Department of Pharmacology and Toxicology, College of Pharmacy, University of Hail, P. O. Box 2440, 81451 Hail, Saudi Arabia
Department of Clinical Pharmacology, College of Pharmacy, University of Hail, P. O. Box 2440, 81451 Hail, Saudi Arabia
Department of Chemistry and Molecular Biology, University of Gothenburg, 40530 Gothenburg, Sweden
Computational Chemistry and Biology Group, Facultad de Química, UdelaR, 11800 Montevideo, Uruguay
Author to whom correspondence should be addressed.
Academic Editor: Derek J. McPhee
Received: 17 February 2016 / Revised: 7 March 2016 / Accepted: 9 March 2016 / Published: 15 March 2016
(This article belongs to the Special Issue Computational Design: A New Approach to Drug and Molecular Discovery)
View Full-Text   |   Download PDF [7066 KB, uploaded 15 March 2016]   |  


A new CYP26A1 homology model was built based on the crystal structure of cyanobacterial CYP120A1. The model quality was examined for stereochemical accuracy, folding reliability, and absolute quality using a variety of different bioinformatics tools. Furthermore, the docking capabilities of the model were assessed by docking of the natural substrate all-trans-retinoic acid (atRA), and a group of known azole- and tetralone-based CYP26A1 inhibitors. The preferred binding pose of atRA suggests the (4S)-OH-atRA metabolite production, in agreement with recently available experimental data. The distances between the ligands and the heme group iron of the enzyme are in agreement with corresponding distances obtained for substrates and azole inhibitors for other cytochrome systems. The calculated theoretical binding energies agree with recently reported experimental data and show that the model is capable of discriminating between natural substrate, strong inhibitors (R116010 and R115866), and weak inhibitors (liarozole, fluconazole, tetralone derivatives). View Full-Text
Keywords: CYP26A1; homology model; RAMBA; retinoic acid; molecular docking CYP26A1; homology model; RAMBA; retinoic acid; molecular docking

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Awadalla, M.K.A.; Alshammari, T.M.; Eriksson, L.A.; Saenz-Méndez, P. Improved Homology Model of the Human all-trans Retinoic Acid Metabolizing Enzyme CYP26A1. Molecules 2016, 21, 351.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics



[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top