Researchers have discovered a new way for insulin to interact with its receptor.

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since the discovery of insulin nearly 1 years ago, scientists have been exploring how insulin interacts with its receptor, so as to improve the ability of therapeutic insulin to imitate the working mode of insulin in the body. In a new study, researchers solved the key part of the puzzle by showing how insulin interacts with its receptor at the second binding site. A team of scientists from Paul Langerhans Institute in Dresden and Karl Gustav Carlos from TU Medical College in Dresden, Germany, as well as colleagues from Max Planck Institute in biochemistry at McGill University in Canada in Munich, Germany, and Helsinki University in Finland will publish their research results in the Journal of Chinese Cell Biology on November 14, 219.

Previous studies have introduced the core role of insulin as a blood glucose regulator in detail, and proved that insulin is involved in diabetes and other chronic diseases, including neurodegeneration and cancer. The biological action of insulin is mediated by its receptor-insulin receptor, which is located on the cell surface.

Dr. p>nal explained that when insulin was first administered to patients in the 192s, it was a real breakthrough in the treatment of diabetes. However, it is still challenging to produce insulin that can summarize all endogenous insulin effects. Coskun, head of islet research institute, and Paul Langerhans, partner of German Diabetes Research Center, institute Dresden. The main reason for this is that we don't know how insulin binds to its receptor and how this signal is transmitted in cells.

4 years ago, it was first proposed to combine insulin with two different parts of the receptor. Although we know a lot about the interaction that happened in the first of these sites, we know little about what happened in the second site. Understanding the different ways in which insulin interacts with its receptor will enable researchers to design improved treatments for insulin-related diseases.

In this new study, the Cryo-EM structure of the extracellular domain of insulin receptor, which is intact and saturated with ligands, shows how insulin binds to site 2. Using a powerful technology called cryoelectron microscope, researchers can get detailed 3D pictures of insulin. The extracellular domain of insulin receptor binds to insulin.

* * of Paul Langerhans Institute and German Research Center, together with lead author Dr. Tricia guttmann, explained that the key is to check the external or extracellular domain of insulin receptor after saturation with high concentration of insulin. Diabetes research.

* * from the Department of Structural Cell Biology of Max Planck Institute of Biochemistry and Dr. IngmarSchfer, the first author, added: We have recorded more than 8, electron microscope images and analyzed more than 3, single receptor particles, from which we can generate 2D images of T-shaped complexes and reconstruct 3D images.

This method enables researchers to directly observe the binding of insulin to site 2 for the first time, and shows how the insulin receptor changes its conformation to form a T-shaped structure. The receptor consists of two identical parts, each part contains two insulin binding sites, so a receptor can bind up to four insulin molecules.

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