Paper Citing NAMD - Abstract
Duddela, Srikanth; Sekhar, P. Nataraj; Padmavati, G. V.; Banerjee, Amit Kumar; Murty, U. S. N.
Probing the structure of human glucose transporter 2 and analysis of protein ligand interactions
MEDICINAL CHEMISTRY RESEARCH, 19:836-853, NOV 2010
Diabetes is a metabolic disorder that has emerged recently as a major cause of global concern. Regulation of the blood glucose concentration is essential to maintain the homeostasis. GLUT2, a carrier protein, plays an important role in transporting sugar molecules across the membrane. To understand the function of this carrier molecule, knowledge of its three-dimensional structure is of paramount importance. Homology modeling approach was adopted to decipher the three-dimensional structure and features of human GLUT2. Ninety-eight percent residues of the modeled structure lie in the allowed region of the Ramachandran plot and a RMSD of 0.86 with the template molecule confirms the reliability of the modeled structure. Comparative transmembrane helix prediction from primary sequence as well as analysis of model revealed presence of 12 helices, which is in agreement with the available literature. Molecular mechanical calculations and docking analysis were performed for the selected 33 compounds. Results showed Glipizide as the best interacting ligand based on the fitness values scored from the binding affinity and minimized energy of the docked complex. These results will aid in efficient designing of inhibitor molecules to curb diabetes.
