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Göteborgs universitets publikationer

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

Författare och institution:
M. K. A. Awadalla (-); T. M. Alshammari (-); Leif A Eriksson (Institutionen för kemi och molekylärbiologi); P. Saenz-Mendez (-)
Publicerad i:
Molecules, 21 ( 3 )
ISSN:
1420-3049
Publikationstyp:
Artikel, refereegranskad vetenskaplig
Publiceringsår:
2016
Språk:
engelska
Fulltextlänk:
Sammanfattning (abstract):
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).
Ämne (baseras på Högskoleverkets indelning av forskningsämnen):
NATURVETENSKAP ->
Kemi
Nyckelord:
CYP26A1, homology model, RAMBA, retinoic acid, molecular docking, human cytochrome-p450, blocking-agents, in-vitro, identification, docking, binding, simulations, inhibitors, expression, proteins, Chemistry
Postens nummer:
237501
Posten skapad:
2016-06-09 15:25

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