Universität zu Köln

Wiedemann, Christoph, Voigt, Johanna, Jirschitzka, Jan ORCID: 0000-0003-1007-4700, Haefner, Sabine, Ohlenschlaeger, Oliver and Bordusa, Frank . Backbone and nearly complete side-chain chemical shift assignments of the human death-associated protein 1 (DAP1). Biomol. NMR Assign.. DORDRECHT: SPRINGER. ISSN 1874-270X

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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 H-1, C-13, and N-15 chemical shift assignments of the human DAP1. The limited spectral dispersion, mainly in the H-1(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.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Wiedemann, Christoph UNSPECIFIED UNSPECIFIED UNSPECIFIED Voigt, Johanna UNSPECIFIED UNSPECIFIED UNSPECIFIED Jirschitzka, Jan UNSPECIFIED orcid.org/0000-0003-1007-4700 UNSPECIFIED Haefner, Sabine UNSPECIFIED UNSPECIFIED UNSPECIFIED Ohlenschlaeger, Oliver UNSPECIFIED UNSPECIFIED UNSPECIFIED Bordusa, Frank UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-308809
DOI:	10.1007/s12104-020-09988-x
Journal or Publication Title:	Biomol. NMR Assign.
Publisher:	SPRINGER
Place of Publication:	DORDRECHT
ISSN:	1874-270X
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language Biophysics; Spectroscopy Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/30880