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Multiple WW domains of Nedd4-1 undergo conformational exchange that is quenched upon peptide binding.
- Source :
-
FEBS Letters . Jun2017, Vol. 591 Issue 11, p1573-1583. 11p. - Publication 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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 00145793
- Volume :
- 591
- Issue :
- 11
- Database :
- Academic Search Index
- Journal :
- FEBS Letters
- Publication Type :
- Academic Journal
- Accession number :
- 123542982
- Full Text :
- https://doi.org/10.1002/1873-3468.12664