Publication Type : Journal Article
Publisher : Taylor & Francis
Source : Journal of Biomolecular Structure and Dynamics, Taylor & Francis, Volume 26, Number 4, p.455–464 (2009)
Campus : Amritapuri
School : School of Biotechnology
Department : biotechnology
Year : 2009
Abstract : GLUT4 is a 12 transmembrane (TM) protein belonging to the Class I facilitated glucose transporter family that transports glucose into the cells in an insulin regulated manner. GLUT4 plays a key role in the maintenance of blood glucose homeostasis and inhibition of glucose transporter activity may lead to insulin resistance, hallmark of type 2 diabetes. No crystal structure data is available for any members of the facilitated glucose transporter family. Here, in this paper, we have generated a homology model of GLUT4 based on experimental data available on GLUT1, a Class I facilitated glucose transporter and the crystal structure data obtained from the Glycerol 3-phosphate transporter. The model identified regions in GLUT4 that form a channel for the transport of glucose along with the substrate interacting residues. Docking and electrostatic potential data analysis of GLUT4 model has mapped an ATP binding region close to the binding site of cytochalasin B and genistein, two GLUT4 inhibitors, and this may explain the mechanism by which these inhibitors could potentially affect the GLUT4 function.
Cite this Research Publication : S Suma Mohan, J Jefferson P Perry, Ninu Poulose, Dr. Bipin G. Nair, and Anilkumar Gopalakrishnapillai, “Homology modeling of GLUT4, an insulin regulated facilitated glucose transporter and docking studies with ATP and its inhibitors”, Journal of Biomolecular Structure and Dynamics, vol. 26, pp. 455–464, 2009