Australia is facing an increasing epidemic of type 2 diabetes. There are now approximately 1 million people living with diabetes and around 100,000 new diagnoses each year. Obesity is thought to be the primary cause of type 2 diabetes in people who are genetically predisposed. In part one we explained how inflammation in type 2 diabetes destroys the pancreas tissue and dramatically decreases insulin production. Here we described the insulin receptor in type 2 diabetes. What we have discovered is the molecular detail of how the hormone insulin binds to its so-called receptor protein on the surface of a cell and instructs that cell to take up glucose from the blood and to store it as an energy source. The receptor itself actually spans the cell membrane so it has a part outside, a part inside and insulin binds to the part that is outside. Instant is a small molecule whose structure is determined a long time ago in 1969 but it's been unknown how it interacts with the receptor and that is what we have discovered and its interaction I've characterized as a molecular handshake as the two proteins docked together. When insulin binds to the outside parts of the receptor it brings the two halves of the receptor together and at the same time the two parts inside of the cell unwind and make contact. These two proteins then activate each other. This activation allows the insulin signal to enter the cell. Specialized proteins interact with the activated receptor just below the cell's surface. The receptor activates these proteins and they in turn are able to activate multiple other proteins in a long signal cascade. This complex signaling process eventually tells the cell to take up glucose for use as an energy source. The long signal cascade allows tight control of the signaling process as it can be turned on or off at many different points along the way. In time to your diabetes we believe insulin binds to its receptor normally but the signal is not sent into the cell and the signal cascade does not develop. This is known as insulin resistance. This means that glucose cannot enter the cell and blood glucose remains high. Over time high glucose levels damage many different organs. Insulin as you know has been used to treat diabetes for a very long time. But all of those formulations and types of insulin that have been used in the diabetes context have been designed and formulated without any knowledge of the way in which insulin actually interacts with the receptor. Now for the first time we've got a picture of that and we can use that into the design of new insulins that could be used for the treatment of diabetes. So we could imagine for example the design of instance that act for longer period of time, design of instance that act more quickly, design of instance that are more stable upon storage and that's where we'd like to go with our discovery.