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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
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author Panwalkar, Vineet
Schulte, Marianne
Lecher, Justin
Stoldt, Matthias
Willbold, Dieter
Dingley, Andrew J
author_facet Panwalkar, Vineet
Schulte, Marianne
Lecher, Justin
Stoldt, Matthias
Willbold, Dieter
Dingley, Andrew J
author_sort Panwalkar, Vineet
collection PubMed
description 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.
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spelling pubmed-49364992016-07-14 Data describing the solution structure of the WW3* domain from human Nedd4-1 Panwalkar, Vineet Schulte, Marianne Lecher, Justin Stoldt, Matthias Willbold, Dieter Dingley, Andrew J Data Brief Data Article 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. Elsevier 2016-06-22 /pmc/articles/PMC4936499/ /pubmed/27419198 http://dx.doi.org/10.1016/j.dib.2016.06.024 Text en © 2016 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Data Article
Panwalkar, Vineet
Schulte, Marianne
Lecher, Justin
Stoldt, Matthias
Willbold, Dieter
Dingley, Andrew J
Data describing the solution structure of the WW3* domain from human Nedd4-1
title Data describing the solution structure of the WW3* domain from human Nedd4-1
title_full Data describing the solution structure of the WW3* domain from human Nedd4-1
title_fullStr Data describing the solution structure of the WW3* domain from human Nedd4-1
title_full_unstemmed Data describing the solution structure of the WW3* domain from human Nedd4-1
title_short Data describing the solution structure of the WW3* domain from human Nedd4-1
title_sort data describing the solution structure of the ww3* domain from human nedd4-1
topic Data Article
url 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
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