Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain.

ABSTRACT: Atomic resolution characterization of the full-length p53 tetramer has been hampered by its size and the presence of extensive intrinsically disordered regions at both the N and C termini. As a consequence, the structural characteristics and dynamics of the disordered regions are poorly understood within the context of the intact p53 tetramer. Here we apply trans-intein splicing to generate segmentally ¹⁵N-labeled full-length p53 constructs in which only the resonances of the N-terminal transactivation domain (NTAD) are visible in NMR spectra, allowing us to observe this region of p53 with unprecedented detail within the tetramer. The N-terminal region is dynamically disordered in the full-length p53 tetramer, fluctuating between states in which it is free and fully expos

SUBMITTER: Krois AS 

PROVIDER: S-EPMC6275486 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature