Chemical Shift Assignments and Coupling Constants for the rat Nedd4 WWIII domain
- rat ENaC bP2 Peptide Complex

Rat Nedd4 WWIII domain - ENaC bP2 Peptide Complex

Nedd4 is a ubiquitin protein ligase WW domains of Nedd4 bind PY motif-containing regions in target molecules, including ENaC. ENaC is an ameloride-sensitive sodium channel located on the apical membrane of polarized epithelia. Nedd4 WW domains bind ENaC PY motifs and Nedd4 is a suppressor of ENaC that regukates channel stability at the plasma membrane, likely by ubiquitination.

rNedd4 WWIII domain - rENaC bP2 peptide complex

Resonances for the first two residues (GS), which were vector derived, were not observed in HN-detect experiments.

Resonances for the first two residues (GS), which were vector derived, were not observed in HN-detect experiments. Resonances for Ser 607 were obtained from Ha detect experiments.
Residues leu 608 - thr 613 exist in multiple conformations on the NMR timescale due to cis/trans isomerization at the leu 608 - pro 609 and ile - 610 - pro 611 peptide bonds. Only chemical shifts for the major conformer are reported.

13C-hsqc, aliphatic and aromatic regions

15N/13C-edited NOESY-HSQC, 50 ms and 150 ms

13C F1-filtered, F3-edited NOESY-HSQC, 250 ms

Chemical Shift Assignments and Coupling Constants for the
rat Nedd4 WWIII domain - rat ENaC bP2 Peptide Complex

The N-terminal GS sequence is dervied from the pGEX4T2 vector and
is not part of the natural sequence of rat Nedd4.

The N-terminal GS sequence is derived from the pGEX4T2 vector and
is not part of the natural rENaC sequence.

Solution Structure Of The Rnedd4 Wwiii Domain-Renac Bp2 Peptide Complex

epithelial sodium channel, beta subunit [Oryctolagus cuniculus]

Amiloride-sensitive sodium channel subunit beta [Myotis brandtii]

amiloride-sensitive sodium channel subunit beta [Oryctolagus cuniculus]

PREDICTED: amiloride-sensitive sodium channel subunit beta [Myotis brandtii]

PREDICTED: amiloride-sensitive sodium channel subunit beta [Myotis davidii]

PREDICTED: amiloride-sensitive sodium channel subunit beta isoform X1 [Chlorocebus sabaeus]

RecName: Full=Amiloride-sensitive sodium channel subunit beta; AltName: Full=Beta-NaCH; AltName: Full=Epithelial Na(+) channel

Amiloride-sensitive sodium channel subunit beta (Epithelial Na(+) channel subunit beta) (Beta-ENaC) (SCNEB) (Nonvoltage-gated sodium channel 1 subunit beta) (Beta-NaCH)

Information for expression system and pruification are given
in the Methods section of the paper.

The B molecule was produced biosynthetically for samples
where the B molecule was isotopically enriched with 15N/13C
and the W molecule was at natural abundanc.
For the reverse labeling scheme, where the B molecule was
at natural abundance, an identical peptide was synthesized
using standard F-moc chemistry.
Details for purification of the peptide (biosynthetic and
synthetic) are described in the Methods section.

Chemical shifts (1H, 15N and 13C) and coupling constants were measure
for both components (JHNHA, JHAHB, long-range JCC) of the complex and
are reported in this deposition.

equipped with pulsed field gradients and triple resonance
probes with actively shielded z gradients.

Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995).

Johnson, B.A. and Blevins, R.A. J. Biomol. NMR 4, 603-614 (1994).