Backbone and nearly complete side-chain chemical shift assignments of the human death-associated protein 1 (DAP1).
Christoph WiedemannJohanna VoigtJan JirschitzkaSabine HäfnerOliver OhlenschlãgerFrank BordusaPublished in: Biomolecular NMR assignments (2020)
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 [Formula: see text], [Formula: see text], and [Formula: see text] chemical shift assignments of the human DAP1. The limited spectral dispersion, mainly in the [Formula: see text] 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.
Keyphrases
- endothelial cells
- induced pluripotent stem cells
- pluripotent stem cells
- smoking cessation
- oxidative stress
- endoplasmic reticulum stress
- squamous cell carcinoma
- high resolution
- magnetic resonance imaging
- computed tomography
- mass spectrometry
- preterm infants
- small molecule
- emergency department
- risk assessment
- transcription factor
- protein protein
- low birth weight