Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein

• DOI: 10.1038/srep21994
• Publication Date: 2016-02-25T10:29:48Z
• Authors: Angelo Toto; Carlo Camilloni; Rajanish Giri; Maurizio Brunori; Michele Vendruscolo; Stefano Gianni
• Keywords: Intrinsically Disordered Proteins; Folding (DSP implementation); Molecular Recognition

Abstract Intrinsically disordered proteins often become structured upon interacting with their partners. The mechanism of this ‘folding binding’ process, however, has not been fully characterised yet. Here we present a study the folding intrinsically transactivation domain c-Myb (c-Myb) binding its partner KIX. By determining structure transition state for wild-type and three mutational variants KIX, found remarkable plasticity pathway c-Myb. To explain phenomenon, show that is templated by This adaptive behaviour, which occurs heterogeneous nucleation, differs from robust homogeneous nucleation typically observed globular proteins. We suggest may enable to achieve specific reliable multiple partners while avoiding aberrant interactions.