- Author:
Xiuying MAI
1
;
Ping LI
1
;
Liu XU
1
Author Information
- Publication Type:Journal Article
- Keywords: 3D-struture modeling; insulin-like growth factor-I receptor (IGF1R); molecular docking; sequence analysis
- MeSH: Binding Sites; Computational Biology; Humans; Insulin-Like Growth Factor I; MicroRNAs; chemistry; Molecular Docking Simulation; Protein Structure, Secondary; Protein Structure, Tertiary; Receptor, IGF Type 1; chemistry; Signal Transduction
- From: Chinese Journal of Biotechnology 2016;32(5):693-701
- CountryChina
- Language:Chinese
- Abstract: The length of IGF1R 3'UTR is greater than 7 kb. The structure of IGF1R 3'UTR is complex, with multiple binding sites of miRNAs. IGF1R is involved in the regulation of MAPK and PI3K/AKT signaling pathways and theformation and development of tumors. Bioinformatics analysis can reveal the structure features of IGF1R, which provides ideas for further research. The analysis shows that the binding sites between IGF1R and miRNAs have the highest mutation rate in Neuroblastoma. We analyzed the structure of 3'UTR, miRNAs binding sites, physical and chemical properties, hydrophilic-hydrophobic property, glycosylation and phosphorylation sites, secondary structure and tertiary structure modeling of IGF1R. The locations and names of amino acids interacting in IGF1R and IGF1 were obtained by molecular docking. Therefore, if IGF1R 3'UTR is mutated, the capacity of IGF1R combined with miRNAs will reduce and the IGF1R expression will be up-regulated, and the function of miRNAs will be repressed. We can change the sites of IGF1R to combine with IGF1 to repress the function of IGF1R and IGF1. Then the function of IGF1R will be repressed.