This title appears in the Scientific Report :
2018
Please use the identifier:
http://dx.doi.org/10.1002/1873-3468.12664 in citations.
Multiple WW domains of Nedd4-1 undergo conformational exchange that is quenched upon peptide binding
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...
| Personal Name(s): | Panwalkar, Vineet |
|---|---|
| Neudecker, Philipp / Willbold, Dieter / Dingley, Andrew J. (Corresponding author) | |
| Contributing Institute: |
Strukturbiochemie; ICS-6 |
| Published in: | FEBS letters, 591 (2017) 11, S. 1573 - 1583 |
| Imprint: |
Chichester
Wiley
2017
|
| DOI: |
10.1002/1873-3468.12664 |
| PubMed ID: |
28471472 |
| Document Type: |
Journal Article |
| Research Program: |
Soft Matter, Health and Life Sciences |
| Publikationsportal JuSER |
|
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. |