Discriminating binding mechanisms of an intrinsically disordered protein via a multi-state coarse-grained model.

ABSTRACT: Many proteins undergo a conformational transition upon binding to their cognate binding partner, with intrinsically disordered proteins (IDPs) providing an extreme example in which a folding transition occurs. However, it is often not clear whether this occurs via an "induced fit" or "conformational selection" mechanism, or via some intermediate scenario. In the first case, transient encounters with the binding partner favour transitions to the bound structure before the two proteins dissociate, while in the second the bound structure must be selected from a subset of unbound structures which are in the correct state for binding, because transient encounters of the incorrect conformation with the binding partner are most likely to result in dissociation. A particularly interesting situatio

SUBMITTER: Knott M 

PROVIDER: S-EPMC4032430 | biostudies-literature | 2014 May

REPOSITORIES: biostudies-literature