Deciphering opening mechanisms of 14-3-3 proteins.

ABSTRACT: The 14-3-3 proteins are a highly conserved family of regulatory molecules that play crucial roles in various cellular processes. They are known for their ability to bind to phosphorylated serine and threonine residues on target proteins, which allows them to modulate their activity, localization, and stability. In mammals, there are seven known paralogs of 14-3-3 proteins, designated as β, ε, ζ, η, σ, τ, and γ. Each paralog has distinct biological functions and tissue distributions, which allow a diverse range of regulatory roles in cellular processes. The conformational plasticity of 14-3-3s regulates their interaction with protein partners but has not yet been thoroughly characterized. We investigated this topic by classical molecular dynamics simulations and observed how the γ, ε, and ζ

SUBMITTER: Barrera EE 

PROVIDER: S-EPMC11934215 | biostudies-literature | 2025 Apr

REPOSITORIES: biostudies-literature