Conformational Ensemble and Biological Role of the TCTP Intrinsically Disordered Region: Influence of Calcium and Phosphorylation

摘要: The translationally controlled tumor protein (TCTP) is a multifunctional that may interact with many other biomolecules, including itself. experimental determinations of TCTP structure revealed folded core domain and an intrinsically disordered region, which includes the first highly conserved signature, but whose role in functions remains to be elucidated. In this work, we combined NMR experiments MD simulations characterize conformational ensemble loop, presence or not calcium ions without phosphorylation Ser46 Ser64. Our results show these changes electrostatic conditions induce significant shifts its toward structures more less extended loop pulled away against domain. Particularly, impact transient contacts between two signatures protein. Moreover, both theoretical data interface non-covalent dimerization involves second signature suggests region might involved protein-protein interaction. We also hampers formation dimers, likely by favoring competitive binding interface. All together, propose remodeling surface modulate accessibility partners response variety cellular conditions.