Different Oligomeric States of the Tumor Suppressor p53 Show Identical Binding Behavior towards the S100β Homodimer.

ABSTRACT: The tumor suppressor protein p53 is a transcription factor that is referred to as the "guardian of the genome" and plays an important role in cancer development. p53 is active as a homotetramer; the S100β homodimer binds to the intrinsically disordered C-terminus of p53 affecting its transcriptional activity. The p53/S100β complex is regarded as highly promising therapeutic target in cancer. It has been suggested that S100β exerts its oncogenic effects by altering the p53 oligomeric state. Our aim was to study the structures and oligomerization behavior of different p53/S100β complexes by ESI-MS, XL-MS, and SPR. Wild-type p53 and single amino acid variants, representing different oligomeric states of p53 were individually investigated regarding their binding behavior towards S100β. The sto

SUBMITTER: Wei AAJ 

PROVIDER: S-EPMC9400850 | biostudies-literature | 2022 Jun

REPOSITORIES: biostudies-literature