TY  - JOUR
AU  - Panwalkar, Vineet
AU  - Neudecker, Philipp
AU  - Willbold, Dieter
AU  - Dingley, Andrew J.
TI  - Multiple WW domains of Nedd4-1 undergo conformational exchange that is quenched upon peptide binding
JO  - FEBS letters
VL  - 591
IS  - 11
SN  - 0014-5793
CY  - Chichester
PB  - Wiley
M1  - FZJ-2018-06835
SP  - 1573 - 1583
PY  - 2017
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:28471472
UR  - <Go to ISI:>//WOS:000403354400009
DO  - DOI:10.1002/1873-3468.12664
UR  - https://juser.fz-juelich.de/record/857872
ER  -