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Title: Backbone and nearly complete side-chain chemical shift assignments of the human death-associated protein 1 (DAP1)
Author(s): Wiedemann, Christoph
Voigt, Johanna
Jirschitzka, Jan
Häfner, Sabine
Ohlenschläger, Oliver
Bordusa, Frank
Issue Date: 2021
Type: Article
Language: English
Abstract: 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.
Open Access: Open access publication
License: (CC BY 4.0) Creative Commons Attribution 4.0(CC BY 4.0) Creative Commons Attribution 4.0
Sponsor/Funder: Publikationsfonds MLU
Journal Title: Biomolecular NMR Assignments
Publisher: Springer Netherlands
Publisher Place: Dordrecht
Volume: 15
Original Publication: 10.1007/s12104-020-09988-x
Page Start: 91
Page End: 97
Appears in Collections:Open Access Publikationen der MLU

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