Modeling of human P450 oxidoreductase structure by in silico mutagenesis and MD simulation

Flück, Christa E; Mullis, Primus E; Pandey, Amit V (2009). Modeling of human P450 oxidoreductase structure by in silico mutagenesis and MD simulation. Molecular and cellular endocrinology, 313(1-2), pp. 17-22. Shannon: Elsevier Ireland 10.1016/j.mce.2009.09.001

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P450 oxidoreductase (POR) is the obligate electron donor for microsomal cytochrome P450s and mutations in POR cause several metabolic disorders. We have modeled the structure of human P450 oxidoreductase by in silico amino acid replacements in the rat POR crystal structure. The rat POR has 94% homology with human POR and 38 amino acids were replaced to make its sequence identical to human POR. Several rounds of molecular dynamic simulations refined the model and removed structural clashes from side chain alterations of replaced amino acids. This approach has the advantage of keeping the cofactor contacts and structural features of the core enzyme intact which could not be achieved by homology based approaches. The final model from our approach was of high quality and compared well with experimentally determined structures of other PORs. This model will be used for analyzing the structural implications of mutations and polymorphisms in human POR.

Item Type:

Journal Article (Original Article)


04 Faculty of Medicine > Department of Gynaecology, Paediatrics and Endocrinology (DFKE) > Clinic of Paediatric Medicine > Endocrinology/Metabolic Disorders

UniBE Contributor:

Flück Pandey, Christa Emma, Mullis, Primus-Eugen, Pandey, Amit Vikram




Elsevier Ireland




Amit Vikram Pandey

Date Deposited:

04 Oct 2013 15:12

Last Modified:

02 Mar 2023 23:23

Publisher DOI:


PubMed ID:


Web of Science ID:


URI: (FactScience: 196586)

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