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

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)...

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Detalles Bibliográficos
Autores principales: Panwalkar, Vineet, Schulte, Marianne, Lecher, Justin, Stoldt, Matthias, Willbold, Dieter, Dingley, Andrew J
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4936499/
https://www.ncbi.nlm.nih.gov/pubmed/27419198
http://dx.doi.org/10.1016/j.dib.2016.06.024
Descripción
Sumario: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 χ(1) dihedral angles derived from (3)J couplings and molecular dynamics simulations data.