Villigen AG/Zurich — Researchers at the Paul Scherrer Institute (PSI) and the University of Zurich (UZH) have discovered and deciphered the structure of a protein that, among other things, plays a role in tumor growth in half of all melanomas. Researchers are now looking for active compounds that block this structure.
(CONNECT) Researchers at PSI and UZH have paved the way for new cancer therapies that could be used to treat one of the most dangerous forms of cancer: malignant melanoma. They have discovered a previously unknown protein structure, a mutation of the protein called B-Raf.
Half of these tumors—also known as melanomas—and an additional 7 percent of all other types of cancer exhibit a mutation in this protein. "Cancer tumors affected by B-Raf mutations are considered particularly aggressive and difficult to treat," explains Yasushi Kondo of the PSI Center for Life Sciences in a PSI press release. He is also the lead author of the team's study, which has now been published in the journal *Molecular Cell*.
The B-Raf protein is part of a key signaling pathway in all human cells. When it receives the appropriate signal, two B-Raf proteins bind to form what is known as an active dimer, thereby giving the go-ahead for the next switch. If it fails to come on, traffic comes to a stop. Mutated B-Raf bypasses this control mechanism, allowing the tumor to grow unchecked.
During their investigations of the molecular structure of B-Raf dimers at the Swiss Synchrotron Light Source at PSI and at the Diamond Light Source in Didcot, England, as well as their analyses of human cells at the University of Zurich, the scientists discovered a previously unknown form of B-Raf dimers. This is linked to another protein, MEK1. "In this study, we were able to produce, for the first time, a high-resolution visualization of the exact structure of this formation in its active, functional form," said Kondo.
This is helpful in the development of drugs. Because “the more precisely we know the structure of the building blocks, the more precisely we can design active ingredients that are truly compatible.” For this reason, researchers at PSI, with support from the Swiss Cancer Research Foundation, are already searching for molecules that bind to the protein complex that has now been decoded and can thus block the unwanted signal. ce/mm
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