Journal of Bioinformatics, Proteomics and Imaging Analysis
Homology modeling and molecular docking of URAT1 with chemotherapeutic agents in hyperuricemia and gout
- 1State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Culture Collection and Application and Guangdong Open Laboratory of Applied Microbiology, Guangdong Institute of Microbiology, Guangzhou 510070, China
- 2Guangdong Yuewei Edible Fungi Technology Co., Guangzhou 510663, China
- 3Guangzhou Institutes of Biomedicine and Health, Chinese Academy of Sciences, Guangzhou 510530, China
Tianqiao Yong; State Key Laboratory of Applied Microbiology Southern China, Guangdong Provincial Key Laboratory of Microbial Culture Collection and Application and Guangdong Open Laboratory of Applied Microbiology, Guangdong Institute of Microbiology, Guangzhou 510070, China; Tel: 86-20-32059602; Fax: 86-20-32079392; E-mail: email@example.com
Tianqiao Yong., et al. Homology Modeling and Molecular Docking of URAT1 with Chemotherapeutic Agents for Hyperuricemia and Gout (2017) Bioinfo Proteom Img Anal 3(2): 203-209.
© 2017 Tianqiao Yong. This is an Open access article distributed under the terms of Creative Commons Attribution 4.0 International License.
KeywordsURAT1, Homology modeling, Binding affinity, Molecular docking, Hyperuricemia
Uric acid transporter 1 (URAT1), a protein involved in uric acid reabsorption, has been linked to pathogenesis of hyperuricemia and gout. Hence, targeting this protein is essential for improving drug design and preventing adverse interactions. The present study was aimed to build URAT1 3D structures by homology modeling and to examine chemotherapeutic drugs binding to URAT1 and the interactions therein. Based upon BLAST results, glucose transporter GLUT1 (PDB ID: 4PYP) was considered as a template for homology modeling. Homology models were constructed and refined using MODELLER program and validated using PROCHECK in which 99.2% of residues present in the favored regions of the Ramachandran plots. To examine the response of proteins toward various inhibitors, molecular docking study was carried out and binding affinities was evaluated between -151 to -305 kcal/mol using MMGBSA method. Analysis of docked conformers showed that the residues ARG172, ARG325, LYS145 and ARG477 were involved with the most number of interactions with the drugs tested.