Dramatic New Discovery May Lead To Treatment For Celiac Disease

Researchers at Stanford University have discovered an important new structure for a key enzyme associated with celiac disease. In the December 2007 issue of the open-access journal PLoS Biology, Daniel M. Pinkas and his colleagues explain that until now, it’s only been possible to observe the enzyme – transglutaminase 2 -- when it’s inactive, or “closed.” Dr. Pinkas and his team, however, have been able, for the first time, to observe the enzyme in its active, or “open” state. The enzyme is active when it's binding to gluten.

To the scientists' surprise, the shape of the enzyme is dramatically different when it’s active. In their article, the researchers write, “Very few proteins have been observed to undergo this type of large-scale transformation.”

The researchers believe that the changes they observed in the structure of the active enzyme play a role in the early stages of celiac disease. They expect that being able to observe the enzyme in its active state will help them figure out why it induces an autoantibody response in celiac patients.

In fact, the scientists speculate, their discovery may eventually lead to the development of drugs for treating celiac disease.

_{Source: Pinkas DM, Strop P, Brunger AT, Khosla C. Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol. 2007 Dec;5(12):e327.}