title: Analysis of the Interactions Between Thioredoxin and 20 Selenoproteins in Chicken.
abstract: Thioredoxin (Trx) is a small molecular protein with complicated functions in a number of processes, including inflammation, apoptosis, embryogenesis, cardiovascular disease, and redox regulation. Some selenoproteins, such as glutathione peroxidase (Gpx), iodothyronine deiodinase (Dio), and thioredoxin reductase (TR), are involved in redox regulation. However, whether there are interactions between Trx and selenoproteins is still not known. In the present paper, we used a Modeller, Hex 8.0.0, and the KFC2 Server to predict the interactions between Trx and selenoproteins. We used the Modeller to predict the target protein in objective format and assess the accuracy of the results. Molecular interaction studies with Trx and selenoproteins were performed using the molecular docking tools in Hex 8.0.0. Next, we used the KFC2 Server to further test the protein binding sites. In addition to the selenoprotein physiological functions, we also explored potential relationships between Trx and selenoproteins beyond all the results we got. The results demonstrate that Trx has the potential to interact with 19 selenoproteins, including iodothyronine deiodinase 1 (Dio1), iodothyronine deiodinase 3 (Dio3), glutathione peroxidase 1 (Gpx1), glutathione peroxidase 2 (Gpx2), glutathione peroxidase 3 (Gpx3), glutathione peroxidase 4 (Gpx4), selenoprotein H (SelH), selenoprotein I (SelI), selenoprotein M (SelM), selenoprotein N (SelN), selenoprotein T (SelT), selenoprotein U (SelU), selenoprotein W (SelW), selenoprotein 15 (Sep15), methionine sulfoxide reductase B (Sepx1), selenophosphate synthetase 1 (SPS1), TR1, TR2, and TR3, among which TR1, TR2, TR3, SPS1, Sep15, SelN, SelM, SelI, Gpx2, Gpx3, Gpx4, and Dio3 exhibited intense correlations with Trx. However, additional experiments are needed to verify them.
authors.affiliation: College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People's Republic of China.
authors.forename: Qi
authors.initials: Q
authors.lastname: Liu
authors.affiliation: College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People's Republic of China.
authors.forename: Jie
authors.initials: J
authors.lastname: Yang
authors.affiliation: College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People's Republic of China.
authors.forename: Jingzeng
authors.initials: J
authors.lastname: Cai
authors.affiliation: College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People's Republic of China.
authors.forename: Yilin
authors.initials: Y
authors.lastname: Luan
authors.affiliation: College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People's Republic of China.
authors.forename: Hamid
authors.initials: H
authors.lastname: Sattar
authors.affiliation: College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People's Republic of China.
authors.forename: Man
authors.initials: M
authors.lastname: Liu
authors.affiliation: College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People's Republic of China.
authors.forename: Shiwen
authors.initials: S
authors.lastname: Xu
authors.affiliation: College of Veterinary Medicine, Northeast Agricultural University, Harbin, 150030, People's Republic of China. zhangziwei@neau.edu.cn.
authors.forename: Ziwei
authors.identifier: http://orcid.org/0000-0002-5705-4611
authors.initials: Z
authors.lastname: Zhang
mesh_terms: D000818:Animals; D002645:Chickens; D062105:Molecular Docking Simulation; D025941:Protein Interaction Mapping; D051140:Selenoproteins / Q000737:chemistry / Q000378:metabolism*; D013879:Thioredoxins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D051140:Selenoproteins; D013879:Thioredoxins
keywords: Hex; KFC2 Server; Modeller; Selenoproteins; Trx