A structurally heterogeneous transition state underlies coupled binding and folding of disordered proteins.

ABSTRACT: Many intrinsically disordered proteins (IDPs) attain a well-defined structure in a coupled folding and binding reaction with another protein. Such reactions may involve early to late formation of different native structural regions along the reaction pathway. To obtain insights into the transition state for a coupled binding and folding reaction, we performed restrained molecular dynamics simulations using previously determined experimental binding Φ_b values of the interaction between two IDP domains: the activation domain from the p160 transcriptional co-activator for thyroid hormone and retinoid receptors (ACTR) and the nuclear co-activator binding domain (NCBD) of CREB-binding protein, each forming three well-defined α-helices upon binding. These simulations revealed that bot

SUBMITTER: Karlsson E 

PROVIDER: S-EPMC6349112 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature