Backbone and nearly complete side-chain chemical shift assignments of the human death-associated protein 1 (DAP1)

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

Full text not available from this repository.

DOI:10.1007/s12104-020-09988-x

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