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http://dx.doi.org/10.25673/38428
Titel: | Backbone and nearly complete side-chain chemical shift assignments of the human death-associated protein 1 (DAP1) |
Autor(en): | Wiedemann, Christoph Voigt, Johanna Jirschitzka, Jan Häfner, Sabine Ohlenschläger, Oliver Bordusa, Frank |
Erscheinungsdatum: | 2021 |
Art: | Artikel |
Sprache: | Englisch |
Zusammenfassung: | Death-associated protein 1 (DAP1) is a proline-rich cytoplasmatic protein highly conserved in most eukaryotes. It has been reported to be involved in controlling cell growth and migration, autophagy and apoptosis. The presence of human DAP1 is associated to a favourable prognosis in different types of cancer. Here we describe the almost complete 1H, 13C, and 15N chemical shift assignments of the human DAP1. The limited spectral dispersion, mainly in the 1HN region, and the lack of defined secondary structure elements, predicted based on chemical shifts, identifies human DAP1 as an intrinsically disordered protein (IDP). This work lays the foundation for further structural investigations, dynamic studies, mapping of potential interaction partners or drug screening and development. |
URI: | https://opendata.uni-halle.de//handle/1981185920/38671 http://dx.doi.org/10.25673/38428 |
Open-Access: | Open-Access-Publikation |
Nutzungslizenz: | (CC BY 4.0) Creative Commons Namensnennung 4.0 International |
Sponsor/Geldgeber: | Publikationsfonds MLU |
Journal Titel: | Biomolecular NMR Assignments |
Verlag: | Springer Netherlands |
Verlagsort: | Dordrecht |
Band: | 15 |
Originalveröffentlichung: | 10.1007/s12104-020-09988-x |
Seitenanfang: | 91 |
Seitenende: | 97 |
Enthalten in den Sammlungen: | Open Access Publikationen der MLU |
Dateien zu dieser Ressource:
Datei | Beschreibung | Größe | Format | |
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Wiedemann2021_Article_BackboneAndNearlyCompleteSide-.pdf | 1.41 MB | Adobe PDF | Öffnen/Anzeigen |