Comparison and correlation of binding mode of ATP in the kinase domains of Hexokinase family

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Title	Comparison and correlation of binding mode of ATP in the kinase domains of Hexokinase family
Authors	Yellapu Nanda Kumar¹, Pasupuleti Santhosh Kumar², Gopal Sowjenya², Valasani Koteswara Rao³, Sthanikam Yeswanth², Uppu Venkateswara Prasad², Jangampalli Adi Pradeepkiran¹, PVGK Sarma² & Matcha Bhaskar¹*
Affiliation	¹Division of Animal Biotechnology, Department of Zoology, Sri Venkateswara University, Tirupati, Andhra Pradesh, India-517502; ²Department of Biotechnology, Sri Venkateswara Institute of Medical Sciences, Tirupati, AP, India-517507; ³Department of Pharmacology and Toxicology, University of Kansas, Lawrence, KS 66047, USA.
Email	matchabhaskar2010@gmail.com; *Corresponding author
Article Type	Hypothesis
Date	Received June 09, 2012; Accepted June 11, 2012; Published June 28, 2012
Abstract	Hexokinases (HKs) are the enzymes that catalyses the ATP dependent phosphorylation of Hexose sugars to Hexose-6-phosphate (Hex-6-p). There exist four different forms of HKs namely HK-I, HK-II, HK-III and HK-IV and all of them share a common ATP binding site core surrounded by more variable sequence that determine substrate affinities. Although they share a common binding site but they differ in their kinetic functions, hence the present study is aimed to analyze the binding mode of ATP. The analysis revealed that the four ATP binding domains are showing 13 identical, 7 similar and 6 dissimilar residues with similar structural conformation. Molecular docking of ATP into the kinase domains using Molecular Operating Environment (MOE) soft ware tool clearly showed the variation in the binding mode of ATP with variable docking scores. This probably explains the variable phosphorylation rates among hexokinases family.
Keywords	Hexokinase, Molecular Docking, MOE
Citation	*Kumar et al.* Bioinformation 8(12): 543-547 (2012)
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.