UB-lead study, cover of the journal ʻStructureʼ
Deregulation of protein c-Src is directly involved in colorectal cancer and other oncological processes, like metastasis survival. The first eighty-five remains of this protein do not adopt a defined structure, so it was thought that they were not important in terms of function.
Deregulation of protein c-Src is directly involved in colorectal cancer and other oncological processes, like metastasis survival. The first eighty-five remains of this protein do not adopt a defined structure, so it was thought that they were not important in terms of function.
By using the resources provided by nuclear magnetic resonance, a technique in which the UB is pioneer, the Research Group Biomolecular Nuclear Magnetic Resonance (BIO-RMN) —led by Miquel Pons and affiliated with the Department of Organic Chemistry of the UB— has just published an article that describes how disordered unique domain of c-Src, despite its great flexibility, interacts with neighbour domains and enables to integrate different types of signals to modulate c-Src response.
The study, highlighted on the cover of Structureʼs May issue, “first proves how different c-Src regulation mechanisms are integrated and it provides new insights into treatment development”, affirms Miquel Pons, professor of Organic Chemistry. The study has been funding by the La Marató de TV3 Foundation and the Spanish Ministry of Economy and Competitiveness.
The blog of the journal editor also highlights the study on an interview to UB researchers Miquel Pons and Mariano Maffei, trainee researcher and first author of the article.
Article reference:
Maffei, M.; Arbesú, M.; Le Roux, A.-L.; Amata, I.; Roche, S.; Pons, M. "The SH3 domain acts as a scaffold for the N-terminal intrinsically disordered regions of c-Src". Structure, May 2015. Doi: 10.1016/j.str.2015.03.009