Insilico Analysis of Fmrp Protein in Fragile X SyndromePriya Durairaj, Rohithkumar Reddy, Thirunavukkarasu Palaniyandi, Rajeswari Hari and Saravanan T. S.
Department of Biotechnology, Dr. M.G.R Educational and Research Institute University, Maduravoyal, Chennai-95, India.
Corresponding Author E-mail: email@example.com
Abstract: To evaluate the effect of mutation in FMR1 protein on the binding energy of protein interaction by homology modeling and docking study using Bioinformatics approach. As per NCBI/Swiss Prot database information normal and mutated FMR1 proteins with accession number AAB28395 and rs121434622, respectively and interacting proteins Cytoplasmic FMR-1 interacting protein, Cytoplasmic FMR1 interacting protein 2, Pre mRNA 3’- end- processing, Tudor domain-containing protein3 (TDRD3), Kinesin like protein KIF3C (KIF3C) and Microspherule protein 1 (MCRS1) has been modeled by using the web server MODWEB for tertiary structures and thereafter every interacting protein was allowed to dock with normal and mutated FMR1 protein by involving HEX server to record the changes in binding energy resultant of mutation. Based on the homology modeling approach, tertiary structures of all studied proteins were successfully modeled and further in docking analysis it has been observed that mutated FMR1 protein highlighted decreased change in the binding energy as compared to normal FMR1 protein docking. Based on the bioinformatics approaches, our study confirms that lowering change in the binding energy for the interacting protein with mutated FMR1 protein when compared to normal FMR1 protein does clearly affect the protein - protein interaction and hence it lead to Fragile X syndrome in affected patients showcasing such mutations.Keywords: FMR1; Fragile X Syndrome; Protein Docking; Binding Energy; Protein Interaction Back to TOC