Multiple WW domains of Nedd4-1 undergo conformational exchange that is quenched upon peptide binding.

The third WW domain (WW3*) of the ubiquitin ligase human neuronal precursor cell expressed developmentally downregulated gene 4-1 (hNedd4-1) was reported to bind its PY motif peptide by a coupled folding-binding equilibrium. However, it is unknown whether these thermodynamic properties are retained in the context of neighboring hNedd4-1 domains. In ...
this report, NMR data show that the WW3* displays a fold-unfold equilibrium in the presence of neighboring WW domains, and that similar fold-unfold equilibria also likely exist for neighboring WW domains. These equilibria are quenched upon interaction with peptide. Thus, the binding mechanism of hNedd4-1 WW domains to proteins involves coupled folding and binding equilibria, and this mechanism may be a general feature that modulates peptide affinities of WW domains.
Mesh Terms:
Amino Acid Sequence, Endosomal Sorting Complexes Required for Transport, Humans, Magnetic Resonance Spectroscopy, Molecular Sequence Data, Nedd4 Ubiquitin Protein Ligases, Open Reading Frames, Peptides, Protein Binding, Protein Domains, Ubiquitin-Protein Ligases
FEBS Lett.
Date: Dec. 01, 2016
Download Curated Data For This Publication
211767
Switch View:
  • Interactions 1