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  • Veronique Receveur-Brechot, DR2 CNRS
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    Our group is mainly interested on deciphering the structural and functional properties of intrinsically disordered proteins involved in human pathologies and particularly in cancers. During the last decade, a growing interest has focused on these particularly intriguing proteins, as they are functionally active, despite their lack of stable regular structure. Intrinsically disordered regions can act as spacers to modulate the distance and the activity of different modules, such as in cellulases.

    Others are involved in many molecular recognition processes that play crucial roles in the mechanisms of regulation of the cell cycle. These latter proteins are called hubs because they can interact with many different partners and are implicated in a large network of interactions. No less than 30% of the proteins encoded in the human genome contain long disordered regions and they are found in numerous cancer-related processes. Interaction with their partners often leads to a gain in secondary structure, a process called induced folding. We have developed an expertise in the study of these original proteins and of their mechanisms of action by combining a series of complementary biophysical techniques.

    We are in particular expert in Small Angle X-ray Scattering (SAXS), a very powerful technique that can provide crucial information on the conformational properties of flexible polypeptide chains and on their distribution of conformations. We also develop projects on globular well folded complexes that are reluctant to crystallization. Here again, we use SAXS, in combination with atomic structures from crystallography or NMR, and with molecular dynamics, to assess the structure of various proteins, involved in macromolecular assemblies, or that undergo conformational changes upon interaction with a substrate, an inhibitor, a cofactor, etc.


    Publications in journals for the General Public