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000857872 1001_ $$0P:(DE-Juel1)157799$$aPanwalkar, Vineet$$b0
000857872 245__ $$aMultiple WW domains of Nedd4-1 undergo conformational exchange that is quenched upon peptide binding
000857872 260__ $$aChichester$$bWiley$$c2017
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000857872 520__ $$aThe 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.
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000857872 7001_ $$0P:(DE-Juel1)144510$$aNeudecker, Philipp$$b1
000857872 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b2
000857872 7001_ $$0P:(DE-Juel1)145681$$aDingley, Andrew J.$$b3$$eCorresponding author
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