Title

Authors

Affiliation

Department of Bioinformatics, School of Biotechnology and Health Sciences, Karunya University, Coimbatore -641114, Tamil Nadu, India

Email

sureshbio@gmail.com; *Corresponding author

Article Type

Database

Date

Received October 08, 2011; Accepted October 11, 2011; Published October 14, 2011

Cytochrome P450s are superfamily of heme proteins which generally monooxygenate hydrophobic compounds. The human cytochrome P450 4F22 (CYP4F22) was categorized into orphan CYPs because of its unknown function. CYP4F22 is a potential drug target for cancer therapy. However, three-dimensional structure, the active site topology and substrate specificity of CYP4F22 remain unclear. In this study, a three-dimensional model of human P450 4F22 was constructed by comparative modeling using Modeller 9v5. The resulting model was refined by energy minimization subjected to the quality assessment from both geometric and energetic aspects and was found to be of reasonable quality. Docking approach was employed to dock arachidonic acid into the active site of CYP4F22 in order to probe the ligand-binding modes. As a result, several key residues were identified to be responsible for the binding of arachidonic acid with CYP4F22. These findings provide useful information for understanding the biological roles of CYP4F22 and structure-based drug design.

Keywords

Human Cytochrome, P450 4F22, CYP4F22, comparative modeling, molecular docking, arachidonic acid, ligand binding site, 2D QSAR

Citation

Kumar. Bioinformation 7(4): 207-210 (2011)
 

Edited by

P Kangueane

ISSN

0973-2063

Publisher

Biomedical Informatics

License

This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.