Computational Molecular Analysis of Human Rhodopsin, Transducin and Arrestin Interactions: An Insight into Signal Transd
Retinal G-protein receptor; rhodopsin upon light-activation, gets phosphorylated, experiences conformational shift and interacts with G-protein; transducin. To completely obstruct the signal transduction visual protein; arrestin binds consecutively to dis
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Abstract Retinal G-protein receptor; rhodopsin upon light-activation, gets phosphorylated, experiences conformational shift and interacts with G-protein; transducin. To completely obstruct the signal transduction visual protein; arrestin binds consecutively to disrupt the cationic channels of plasma membrane. Experimented binding assays documents the protein interactions but hitherto computational investigation was undone. This probe aims at the computational study of conformational alterations in rhodopsin upon sequential interactions, accompanied by variations in its surface electrostatic potential and net solvent accessible area. 3D structures of human transducin, arrestin and rhodopsin were analyzed. Residual participation from the optimized and simulated trio-complex (rhodopsintransducin-arrestin) disclosed that predominantly positively charged amino-acid residues; Arg474, Arg412, Arg229, Arg13, Lys15 and Lys408 from rhodopsin participated with transducin and arrestin forming 9 ionic interactions. Rhodopsin was perceived to interact in a gradual firmer pattern with its partner proteins. This study presents a novel viewpoint into the computational disclosure for participation of concerned visual proteins.
Tanushree Mukherjee and Arundhati Banerjee are equal contributor. Tanushree Mukherjee ⋅ Sujay Ray (✉) Department of Biotechnology, Bengal College of Engineering & Technology, Durgapur, India e-mail: [email protected] Tanushree Mukherjee e-mail: [email protected] Arundhati Banerjee Department of Biotechnology, National Institute of Technology, Durgapur, India e-mail: [email protected] Sujay Ray Department of Biochemistry and Biophysics, University of Kalyani, Kalyani, Nadia, India © Springer Science+Business Media Singapore 2017 J.K. Mandal et al. (eds.), Proceedings of the First International Conference on Intelligent Computing and Communication, Advances in Intelligent Systems and Computing 458, DOI 10.1007/978-981-10-2035-3_4
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Keywords Homology modeling Optimized Rhodopsin-Transducin-Arrestin complex Protein-protein interactions Conformational switches Stability and simulation
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Abbreviations MD P.I.C. S1 S2 S3
Molecular Dynamics Protein Interaction Calculator Rhodopsin before any Interaction Rhosopsin after Interaction with Transducin Rhodopsin after Interaction with Arrestin in presence of Transducin
1 Introduction In darkness or dim light, the rod cells take the active responsibility for the human vision. One such associated vital protein; human rhodopsin is a retinal G-protein receptor that is present in the rod cells and is responsible for the photo transduction process. Light activates the rhodopsin which then undergoes conformational alterations [1, 2]. Due to this conformational shift in rhodopsin, a G-protein; transducin gets instantly triggered to interact with the altered rhodopsin [1, 2]. Binding assay studies from earlier investigations suggests that the α-subunit of transducin now binds to rhodopsin at a definite binding site
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