Diabetes is a disease that affects millions of Americans every day. As the years go by, diabetes is becoming more and more common in America. Research is underway to gain valuable information about the disease and to develop treatments for the disease. There are several causes of diabetes, but each involves contact with insulin and the insulin receptor at some level, since insulin and the insulin receptor are involved in the pathway that regulates glucose levels within the body. The insulin/insulin receptor pathway is vital to maintaining homeostasis within the body. As more information is gathered about the structure of the insulin receptor and how it works, a better understanding of diabetes treatments may be gained. Insulin Receptor Gene The insulin receptor has several defined exons that code for various regions of the protein, and knowledge of this information begins to allow for a greater understanding of the structure of the insulin receptor. Insulin receptor formation begins through proteolytic cleavage of the insulin receptor zymogen (Seino et al., 1989). The insulin receptor is a homodimeric protein with α2β2 subunits (Huang et al., 2004). From cDNA analysis, it was found that eleven exons constitute the α subunit and 11 exons constitute the β subunit (Seino et al., 1989). These exons lead to the specific characteristics that the insulin receptor displays within its structure. General Structure There is a lot of research on the structure of the insulin receptor because it has many vital functions within the body and because of its function or lack of function in such a widespread disease as diabetes. As mentioned before, the insulin receptor is a homodimeric protein containing two α and two...... middle of paper...... MC How insulin engages its primary binding site on the insulin receptor . Nature, 493: 241-248 (2013) Olefsky, J. The insulin receptor: a multifunctional protein. Diabetes, 39: 1009-1016 (1990)Schaffer, L.; A model for the binding of insulin to the insulin receptor. European Journal of Biochemistry, 221:1127-1132 (1994)Seino, S.; Seino, M.; Nishi, S.; Bell, G. Structure of the human insulin receptor gene and characterization of its promoter. Proceedings of the National Academy of Sciences USA, 86: 114-118 (1989) Smith, B.J.; Huang, K.; Kong, G.; Chan, S.J.; Nakagawa, S.; Menting, J.G.; Hu, S.; Whittaker, J.; Steiner, D.F.; Katsoyannis, PG Structural resolution of a tandem hormone-binding element in the insulin receptor and its implications for the design of peptide agonists. Proceedings of the National Academy of Sciences, 107(15): 6771-6776 (2010)