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| 001 | 857872 | ||
| 005 | 20210129235748.0 | ||
| 024 | 7 | _ | |a 10.1002/1873-3468.12664 |2 doi |
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| 100 | 1 | _ | |a Panwalkar, Vineet |0 P:(DE-Juel1)157799 |b 0 |
| 245 | _ | _ | |a Multiple WW domains of Nedd4-1 undergo conformational exchange that is quenched upon peptide binding |
| 260 | _ | _ | |a Chichester |c 2017 |b Wiley |
| 336 | 7 | _ | |a article |2 DRIVER |
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| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1544530404_28834 |2 PUB:(DE-HGF) |
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| 336 | 7 | _ | |a Journal Article |0 0 |2 EndNote |
| 520 | _ | _ | |a 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. |
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| 700 | 1 | _ | |a Neudecker, Philipp |0 P:(DE-Juel1)144510 |b 1 |
| 700 | 1 | _ | |a Willbold, Dieter |0 P:(DE-Juel1)132029 |b 2 |
| 700 | 1 | _ | |a Dingley, Andrew J. |0 P:(DE-Juel1)145681 |b 3 |e Corresponding author |
| 773 | _ | _ | |a 10.1002/1873-3468.12664 |g Vol. 591, no. 11, p. 1573 - 1583 |0 PERI:(DE-600)1460391-3 |n 11 |p 1573 - 1583 |t FEBS letters |v 591 |y 2017 |x 0014-5793 |
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