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| Hauptseite > Publikationsdatenbank > The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria. > print |
| Hauptseite > Publikationsdatenbank > The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria. > print |
| 001 | 283504 | ||
| 005 | 20210129222329.0 | ||
| 024 | 7 | _ | |a 10.1021/acs.biochem.5b01028 |2 doi |
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| 100 | 1 | _ | |a Panwalkar, Vineet |0 P:(DE-Juel1)157799 |b 0 |u fzj |
| 245 | _ | _ | |a The Nedd4-1 WW Domain Recognizes the PY Motif Peptide through Coupled Folding and Binding Equilibria. |
| 260 | _ | _ | |a Columbus, Ohio |c 2016 |b American Chemical Society |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1457439698_1124 |2 PUB:(DE-HGF) |
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| 520 | _ | _ | |a The four WW domains of human Nedd4-1 (neuronal precursor cell expressed developmentally downregulated gene 4-1) interact with the PPxY (PY) motifs of the human epithelial Na(+) channel (hENaC) subunits, with the third WW domain (WW3*) showing the highest affinity. We have shown previously that the α-hENaC PY motif binding interface of WW3* undergoes conformational exchange on the millisecond time scale, indicating that conformational sampling plays a role in peptide recognition. To further understand this role, the structure and dynamics of hNedd4-1 WW3* were investigated. The nuclear Overhauser effect-derived structure of apo-WW3* resembles the domain in complex with the α-hENaC peptide, although particular side chain conformations change upon peptide binding, which was further investigated by molecular dynamics simulations. Model-free analysis of the (15)N nuclear magnetic resonance spin relaxation data showed that the apo and peptide-bound states of WW3* have similar backbone picosecond to nanosecond time scale dynamics. However, apo-WW3* exhibits pronounced chemical exchange on the millisecond time scale that is quenched upon peptide binding. (1)HN and (15)N Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments at various temperatures revealed that apo-WW3* exists in an equilibrium between the natively folded peptide binding-competent state and a random coil-like denatured state. The thermodynamics of the folding equilibrium was determined by fitting a thermal denaturation profile monitored by circular dichroism spectroscopy in combination with the CPMG data, leading to the conclusion that the unfolded state is populated to ∼20% at 37 °C. These results show that the binding of the hNedd4-1 WW3* domain to α-hENaC is coupled to the folding equilibrium. |
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| 700 | 1 | _ | |a Dingley, Andrew J |0 P:(DE-HGF)0 |b 9 |e Corresponding author |
| 773 | _ | _ | |a 10.1021/acs.biochem.5b01028 |g Vol. 55, no. 4, p. 659 - 674 |0 PERI:(DE-600)1472258-6 |n 4 |p 659 - 674 |t Biochemistry |v 55 |y 2016 |x 1520-4995 |
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