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Data describing the solution structure of the WW3* domain from human Nedd4-1.

ABSTRACT: The third WW domain (WW3*) of human Nedd4-1 (Neuronal precursor cell expressed developmentally down-regulated gene 4-1) interacts with the poly-proline (PY) motifs of the human epithelial Na+ channel (hENaC) subunits at micromolar affinity. This data supplements the article (Panwalkar et al., 2015) [1]. We describe the NMR experiments used to solve the solution structure of the WW3* domain. We also present NOE network data for defining the rotameric state of side chains of peptide binding residues, and complement this data with ? 1 dihedral angles derived from (3) J couplings and molecular dynamics simulations data.

SUBMITTER: Panwalkar V

PROVIDER: S-EPMC4936499 | biostudies-literature | 2016 Sep

REPOSITORIES: biostudies-literature

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Data describing the solution structure of the WW3* domain from human Nedd4-1.

Panwalkar Vineet V Schulte Marianne M Lecher Justin J Stoldt Matthias M Willbold Dieter D Dingley Andrew J AJ

Data in brief 20160622

The third WW domain (WW3*) of human Nedd4-1 (Neuronal precursor cell expressed developmentally down-regulated gene 4-1) interacts with the poly-proline (PY) motifs of the human epithelial Na+ channel (hENaC) subunits at micromolar affinity. This data supplements the article (Panwalkar et al., 2015) [1]. We describe the NMR experiments used to solve the solution structure of the WW3* domain. We also present NOE network data for defining the rotameric state of side chains of peptide binding residu ...[more]

PMID: 27419198

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