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International Journal of Computational Bioinformatics and In Silico Modeling
2014: Volume-3 Issue-5
ISSN: 2320-0634

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ABSTRACT   REFERENCES  
International Journal of Computational Bioinformatics and In Silico Modeling 3(5) 2014: 466-472

Structural Characterization of Arg322Gln Mutation in Fat Mass and Obesity Associated Protein



Mazhar Hussain*, Ramla Ashfaq and Syeda Anum Zehra

National Centre of Excellence in Molecular Biology, University of the Punjab, Lahore.

* Corresponding Author

ABSTRACT

Fat mass and obesity associated gene has shown a strong association with adiposity in children and adults during several Genome Wide Association studies. It encodes an enzyme which catalyzes demethylation of single stranded DNA by using 2-oxoglutarate (2-OG) as a co-substrate. A mutation in the N - terminal of the enzyme encodes a glutamine in place of the arginine residue at position 322, which results in a complete disruption of protein function. Sequence analysis Arg322 is a highly conserved amino acid in the Fat mass obesity associated protein in animals. Homology modeling analysis reveals that 2-OG binding site of the enzyme which comprises various amino acids including Arg322. Molecular docking studies showed that Gln322 was unable to develop the hydrogen bonding and electrostatic interaction with the 2-OG. These interactions are important for extending the 2-OG to make its bonds more accessible to other amino acids. This study indicates that Arg322 is one of the most conserved amino acid in FTO protein which is directly involved in the catalysis of the 2-OG to succinate and CO2.

 


Copyright © 2014 | AIZEON publishers | All rights reserved

 

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Citation: Mazhar Hussain et al. (2014). Structural Characterization of Arg322Gln Mutation in Fat Mass and Obesity Associated Protein. Int J Comput Bioinfo In Silico Model 3(5): 466-472

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