While the correct function of many proteins depends on their three-dimensional structure, some appear to adopt random forms. For one of them, a team of researchers at Ruhr-Universität Bochum (RUB) has shown that the supposed disorder is not disorder after all: the protein HMGA1a adopts dynamic, more compact structures that depend on its phosphorylation. A malfunction of HMGA1a can lead to cancer. The researchers led by Profesoor Raphael Stoll therefore expect their results to form a basis for future therapeutic strategies to combat cancers caused by HMGA1a. They report in the journal Nucleic Acids Research on July, 24 2019.
Many -- but not all -- proteins in a living cell have a defined three-dimensional structure, which is absolutely necessary for their correct activity. The interrelationship between the structure and function of proteins is the focus of many research initiatives that extend to the development of innovative drugs.
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"However, based on recent research results, it is predicted that at least 30 per cent of all proteins in cells containing a nucleus are partially or even completely unstructured," says Raphael Stoll, head of the Biomolecular Spectroscopy research group. Despite or precisely because of this remarkable feature, these proteins have special, sometimes crucial, functions in both healthy and disease-causing processes. These include, for example, the regulation of the cell cycle, the transmission of biological signals, and the development of cancer or neurodegenerative diseases such as Alzheimer's or Parkinson's disease.
One of these seemingly disordered proteins is the high-mobility group protein A1a (HMGA1a). It is highly abundant in the...
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