Molecular Recognition by Templated Folding of an Intrinsically Disordered Protein.

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

SUBMITTER: Toto A 

PROVIDER: S-EPMC4766501 | biostudies-literature | 2016 Feb

REPOSITORIES: biostudies-literature