Structural insights and biophysical characterization of p90RSK2:ERK2 complex.

ABSTRACT: Kinase domains are often flanked by flexible tails and intrinsically disordered regions (IDRs) that contain conserved motifs. The co-ordinated action and interplay of IDRs and folded kinase domains is necessary for the proper function of kinases and kinase complexes. Characterization of full-length kinases and complexes is often challenging due to the flexible nature of flanking IDRs, yet necessary to fully understand their function and regulation. The p90 ribosomal S6 kinase (RSK) family is a unique kinase family with two distinct, functional kinase domains (NTK and CTK) flanked by flexible tails and a linker. RSK2 forms a stable complex with its activating kinase, ERK2, and here, we use multiple complementary techniques, hydrogen-deuterium exchange mass spectrometry, cryoelectron microsc

SUBMITTER: Kobori EK 

PROVIDER: S-EPMC12614931 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature