ISSN: 2641-9459
Authors: Michaux C*, Mignon J and Perpète EA
In contrast to the classical paradigm “one sequence -one structure - one function” that a given protein sequence corresponds to a well-defined three-dimensional (3D) structure and an associated function, it was discovered in the 1990s that an increasing number of proteins can be functional in the absence of a stable 3D-structure [1]. This new concept, the “disorder-function paradigm”, assumes that an intrinsically flexible protein may have several structures and consequently various functions. Several terms were used to name these proteins: e.g. intrinsically disordered proteins (IDPs), natively unfolded proteins (NUPs), natively denatured proteins (NDPs) or intrinsically unstructured proteins (IUPs). Whereas some IDPs are predicted to be fully disordered, most of them are also known to have both structured domains and disordered regions.
Keywords: Intrinsically disordered proteins; Therapeutic targets; Drug design; Protein-Protein Interactions
