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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)...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2016
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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 |
_version_ | 1782441571396878336 |
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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. |
format | Online Article Text |
id | pubmed-4936499 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Elsevier |
record_format | MEDLINE/PubMed |
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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