Allosteric Modulation of JNK Docking Site Interactions with ATP-Competitive Inhibitors.

ABSTRACT: The c-Jun N-terminal kinases (JNKs) play a wide variety of roles in cellular signaling processes, dictating important, and even divergent, cellular fates. These essential kinases possess docking surfaces distal to their active sites that interact with diverse binding partners, including upstream activators, downstream substrates, and protein scaffolds. Prior studies have suggested that the interactions of certain protein-binding partners with one such JNK docking surface, termed the D-recruitment site (DRS), can allosterically influence the conformational state of the ATP-binding pocket of JNKs. To further explore the allosteric relationship between the ATP-binding pockets and DRSs of JNKs, we investigated how the interactions of the scaffolding protein JIP1, as well as the upstream activa

SUBMITTER: Lombard CK 

PROVIDER: S-EPMC6338552 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature