Comparison and correlation of binding mode of ATP in the kinase domains of Hexokinase family |
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| Authors: | Yellapu Nanda Kumar Pasupuleti Santhosh Kumar Gopal Sowjenya Valasani Koteswara Rao Sthanikam Yeswanth Uppu Venkateswara Prasad Jangampalli Adi Pradeepkiran Pvgk Sarma Matcha Bhaskar |
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| 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 |
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| 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. |
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| Keywords: | Hexokinase Molecular Docking MOE |
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