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Title

Homology modeling of human serum paraoxonase1 and its molecular interaction studies with aspirin and cefazolin

 

Authors

Mohammed Salman1, 2, Chandramouli Malleda3, Narayanavari A Suneel4, Insaf A Qureshi5, Elizabeth A Frank1, Cletus JM DíSouza1*

 

Affiliation

1Department of studies Biochemistry, University of Mysore, Mysore 570006, India; 2Anthropological survey of India, Southern regional center, Bogadi, Mysore 570006; 3Department of Biochemistry, University of Hyderabad, Hyderabad 500046, India; 4Department of Animal Sciences, University of Hyderabad, Hyderabad 500046, India; 5Department of Biotechnology, University of Hyderabad, Hyderabad 500046, India

 

Email

cletus@biochemistry.uni-mysore.ac.in; *Corresponding author

 

Phone

+91 821 2419621

 

Article Type

Hypothesis

 

Date

Received August 12, 2011; Accepted August 13, 2011; Published September 06, 2011

 

Abstract

Human serum paraoxonase1 (HuPON1) belongs to the family of A-esterases (EC.3.1.8.1). It is associated with HDL particle and prevents atherosclerosis by cleaving lipid hydroperoxides and other proatherogenic molecules of oxidized low density lipoproteins (LDL). Since the precise structure of HuPON1 is not yet available, the structure-function relationship between HuPON1 and activators/inhibitors is still unknown. Therefore, a theoretical model of HuPON1 was generated using homology modelling and precise molecular interactions of an activator aspirin and an inhibitor cefazolin with PON1 were studied using Autodock software. The ligand binding residues were found to be similar to the predicted active site residues. Both cefazolin and aspirin were found to dock in the vicinity of the predicted active sites of PON1; cefazolin bound at residues N166, S193 and Y71, while aspirin at residues N309, I310 and L311. Binding region in the PON1 by prediction (3D2GO server) and docking studies provide useful insight into mechanism of substrate and inhibitor binding to the enzyme active site.

 

Keywords

Human Paraoxonase1; prediction; molecular docking; homology modeling; secondary structure

 

Citation

Salman et al. Bioinformation 7(2): 59-63 (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.