1. Backbone and nearly complete side-chain chemical shift assignments of the human death-associated protein 1 (DAP1)
- Author
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Sabine Häfner, Frank Bordusa, Oliver Ohlenschläger, Christoph Wiedemann, Johanna Voigt, and Jan Jirschitzka
- Subjects
Stereochemistry ,IDP ,Apoptosis ,Spectral dispersion ,Biochemistry ,Article ,Cell growth ,03 medical and health sciences ,0302 clinical medicine ,Structural Biology ,Autophagy ,Side chain ,Cell migration ,Death-associated protein 1 ,Nuclear Magnetic Resonance, Biomolecular ,Protein secondary structure ,resonance assignment ,Cell Proliferation ,030304 developmental biology ,0303 health sciences ,Chemistry ,Chemical shift ,Chemical shifts ,Intrinsically Disordered Proteins ,Death associated protein ,Intrinsically disordered protein ,030220 oncology & carcinogenesis ,Apoptosis Regulatory Proteins ,Human - 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 $${{^{1}}\text {H}}$$ 1 H , $${{^{13}}\text {C}}$$ 13 C , and $${{^{15}}\text {N}}$$ 15 N chemical shift assignments of the human DAP1. The limited spectral dispersion, mainly in the $${{^{1}}\text {H}{^{\text{N}}}}$$ 1 H N 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.
- Published
- 2020