Author(s): A. Ranganadha Reddy, T.C. Venkateswarulu, D. John Babu, N. Shyamala Devi

Email(s): rangaaluri@gmail.com

DOI: Not Available

Address: A. Ranganadha Reddy1*, T.C. Venkateswarulu1, D. John Babu1, N. Shyamala Devi2
1School of Biotechnology, Vignan University, Vadlamudi, Guntur, 522213, India
2Department of Biotechnology, Sree Vidyanikethan Engg. College, Tirupathi, 517102, India
*Corresponding Author

Published In:   Volume - 7,      Issue - 3,     Year - 2014


ABSTRACT:
Alzheimer’s disease is a brain disorder characterized by the most common form of dementia associated with plaques and tangles in the brain. The most commonly recognized symptoms are memory loss, such as difficulty in remembering and occasional problems with remembering certain things and confusion. These symptoms are signs of a failing brain cells. The brain has 100 billion nerve cells (neurons).Each nerve cell communicates with many others to form networks. In Alzheimer’s disease, increasing numbers of brain cells deteriorate as in other types of dementia.Tau-protein kinase (EC 2.7.11.26)is an enzyme that catalyzes the transferring of a phosphate group to the side chain oxygen atom of serine or threonine residues. Tau-protein is an important protein of the central nervous system that stabilizes microtubules and neurons. Abundant neurofibrillary lesions made of hyperphosphorylated Tau-protein constitute one of the defining neuropath logical features of Alzheimer’s disease. Tau-proteins interact with tubulin to stabilize microtubules. Pathogenesis of Alzheimer’s disease includes hyperphosphorylation of the tau-protein which results in the self-assembly of tangles of paired helical fragments and straight filaments. Defective Tau-protein causes the dementia leading to Alzheimer’s disease. Considering the importance and lack of structural information, we modeled Tau protein with homology modeling and performed docking studies with L-Glutamic acid, Memantine, Tacrine, Ropinirol ligand. The minimized modeled structure has shown good structure similarity with template and show high binding association energy with ligand.


Cite this article:
A. Ranganadha Reddy, T.C. Venkateswarulu, D. John Babu, N. Shyamala Devi. Homology Modeling, Simulation and Docking Studies of Tau-Protein Kinase. Research J. Pharm. and Tech. 7(3): Mar., 2014; Page 376-388.


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RNI: CHHENG00387/33/1/2008-TC                     
DOI: 10.5958/0974-360X 

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