Mapping the transition state for a binding reaction between ancient intrinsically disordered proteins.

ABSTRACT: Intrinsically disordered protein domains often have multiple binding partners. It is plausible that the strength of pairing with specific partners evolves from an initial low affinity to a higher affinity. However, little is known about the molecular changes in the binding mechanism that would facilitate such a transition. We previously showed that the interaction between two intrinsically disordered domains, NCBD and CID, likely emerged in an ancestral deuterostome organism as a low-affinity interaction that subsequently evolved into a higher-affinity interaction before the radiation of modern vertebrate groups. Here we map native contacts in the transition states of the low-affinity ancestral and high-affinity human NCBD/CID interactions. We show that the coupled binding and folding mech

SUBMITTER: Karlsson E 

PROVIDER: S-EPMC7762952 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature