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@ARTICLE{Panwalkar:857872,
author = {Panwalkar, Vineet and Neudecker, Philipp and Willbold,
Dieter and Dingley, Andrew J.},
title = {{M}ultiple {WW} domains of {N}edd4-1 undergo conformational
exchange that is quenched upon peptide binding},
journal = {FEBS letters},
volume = {591},
number = {11},
issn = {0014-5793},
address = {Chichester},
publisher = {Wiley},
reportid = {FZJ-2018-06835},
pages = {1573 - 1583},
year = {2017},
abstract = {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.},
cin = {ICS-6},
ddc = {610},
cid = {I:(DE-Juel1)ICS-6-20110106},
pnm = {6215 - Soft Matter, Health and Life Sciences (POF3-621)},
pid = {G:(DE-HGF)POF3-6215},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:28471472},
UT = {WOS:000403354400009},
doi = {10.1002/1873-3468.12664},
url = {https://juser.fz-juelich.de/record/857872},
}