Structure of the transition state for the binding of c-Myb and KIX highlights an unexpected order for a disordered system

• DOI: 10.1073/pnas.1307337110
• Publication Date: 2013-08-27T02:24:39Z
• Authors: Rajanish Giri; Angela Morrone; Angelo Toto; Maurizio Brunori; Stefano Gianni
• Keywords: MYB

A classical dogma of molecular biology dictates that the 3D structure a protein is necessary for its function. However, considerable fraction human proteome, although functional, does not adopt defined folded state under physiological conditions. These intrinsically disordered proteins tend to fold upon binding their partners with mechanism elusive experimental characterization. Indeed, many hypotheses have been put forward, functional role (if any) disorder in these denatured systems still shrouded mystery. Here, we characterize transition binding-induced folding reaction between KIX domain CREB-binding and transactivation c-Myb. The analysis, based on characterization series conservative site-directed mutants, reveals very high content native-like indicates recognition c-Myb geometrically precise. implications our results light previous work unstructured are discussed.