Scientists have described a new family of proteins that appear to play a key role in cancer and might be targets for future cancer drugs.
A major new study in the journal Nature sets out the structure of the new family, called glutamate intramembrane proteases the founding member of which plays a critical role in transforming healthy cells into cancer cells.
The research, funded by Cancer Research UK and conducted by scientists at The Institute of Cancer Research, London, defined the structure of a protein called Rce1, and established it as the first known member of a whole new protein family.
The research was conducted on Methanococcus maripaludis Rce1, a homologue of human Rce1. It has relevance to cancer in humans because Rce1 helps control another class of proteins (the CAAX proteins) involved in cell division and the transformation into cancer.
These CAAX proteins include one of the most important of all triggers for cancer the Ras protein which is enormously important for turning cells cancerous but has been difficult to target with traditional drugs.
Understanding the other proteins that are required for Ras to trigger cancer is therefore enormously important, since they may prove easier targets for precision drug treatment.
The researchers chose M. Maripaludis Rce1 from a shortlist of around 30 versions from different organisms including humans, yeast and bacteria. They selected the M. Maripaludis version as the most suitable for the crystallisation process needed to study the protein in detail. Although M. Maripaludis Rce1 is quite different from human Rce1, it shares important elements of its structure.
Using a second bacterium, Escherichia coli, as a protein factory, the researchers manufactured M. Maripaludis Rce1 before purifying and then crystallising it. Using a technique called X-ray diffraction, they were able to examine the structure of
|Contact: Henry French|
Institute of Cancer Research