In silico modeling and binding energy calculations of thioguanosine and their derivatives against tumor endothelial marker8 Rayalu D. Jayasimha1, Seshapani P.2,*, Kumari J. Pramoda1, Chennaiah K.3, Naidu N.V.1 1Global Institute of Biotechnology, Himayat Nagar, Hyderabad-29, Andhra Pradesh, India 2Department of Microbiolgy, Sri Venkateswara University, P.G Centre, Kavali-524201, Andhra Pradesh, India. 3Department of Zoology, Sri Venkateswara University, P.G Centre, Kavali-524201, Andhra Pradesh, India *Corresponding author: P. Seshapani, Department of Microbiolgy, Sri Venkateswara University, P.G Centre, Kavali-524201, Andhra Pradesh, India
Online published on 26 February, 2013. Abstract Homology modeling of Tumor endothelial marker8 has been performed based on the crystal structure of the 1SHU (Chain X; Crystal Structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor) and by using modeller software. With the aid of the molecular mechanics and molecular dynamics methods, the final model is obtained and is further assessed by procheck and verify 3D graph programs, which showed that the final refined model is reliable. With this model, a flexible docking study of Tumor endothelial marker 8 with a group of thioguanosine derivatives was performed and the results indicated that TYR -21, PHE 22,VAL 158, ASN 159, PHE 162, LEU 165 in Tumor endothelial marker 8 are important determinant residues in binding as they have strong hydrogen bonding with derivatives. These hydrogen binding interactions play an important role for stability of the complex. Among 35 derivatives of thioguanosine, 10th derivative showed best docking result with Tumor endothelial marker8. Our results may be helpful for further experimental investigations. Top Keywords Docking, Homology Modelling, Molecular dynamics, Molecular Mechanics, Tumor endothelial marker8, Thioguanosine. Top |