Metal-coupled folding as the driving force for the extreme stability of Rad50 zinc hook dimer assembly.

ABSTRACT: The binding of metal ions at the interface of protein complexes presents a unique and poorly understood mechanism of molecular assembly. A remarkable example is the Rad50 zinc hook domain, which is highly conserved and facilitates the Zn²⁺-mediated homodimerization of Rad50 proteins. Here, we present a detailed analysis of the structural and thermodynamic effects governing the formation and stability (logK₁₂ = 20.74) of this evolutionarily conserved protein assembly. We have dissected the determinants of the stability contributed by the small β-hairpin of the domain surrounding the zinc binding motif and the coiled-coiled regions using peptides of various lengths from 4 to 45 amino acid residues, alanine substitutions and peptide bond-to-ester perturbations. In the st

SUBMITTER: Kochanczyk T 

PROVIDER: S-EPMC5093744 | biostudies-literature | 2016 Nov

REPOSITORIES: biostudies-literature