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

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Title	Homology modeling of human serum paraoxonase1 and its molecular interaction studies with aspirin and cefazolin
Authors	Mohammed Salman^{1, 2}, Chandramouli Malleda³, Narayanavari A Suneel⁴, Insaf A Qureshi⁵, Elizabeth A Frank¹, Cletus JM D’Souza¹*
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.