A research team from the University of Leicester has provided an opportunity for scientists to develop novel cancer therapeutics, by providing a high-resolution image of a protein linked to several different kinds of cancer.
Cyril Dominguez, who led the work, explained: "My research field is structural biology. The proteins that we have studied, called Sam68 and T-STAR, are very similar and overexpression of Sam68 has been shown to correlate with poor prognosis in many types of cancers.”
Dominguez added, "Our results provide atomic resolution details on how Sam68 binds specifically to its RNA target. Furthermore, we show that Sam68 forms a homodimer that has never been described before and is crucial for its function in RNA splicing.”
This is an important discovery, because this research can now set the stage for future structure-based drug design. If drugs can be designed to bind at the dimerization interface, researchers may be able to prevent the function of these proteins, which could have implications for cancer therapeutics.
Dominguez concluded: "Now that we have a high-resolution structure of Sam68 and T-STAR and a high-throughput binding assay, we are in discussion to collaborate with a major drug discovery consortium to screen a very large library of compounds to inhibit the function of Sam68."
Feracci M, Foot JN, Grellscheid SN et al. Structural basis of RNA recognition and dimerization by the STAR proteins T-STAR and Sam68. Nat Commun, 7 (2016); http://www.eurekalert.org/pub_releases/2016-01/uol-nsc012516.php