Homodimerization of the death-associated protein kinase catalytic domain: development of a new small molecule fluorescent reporter.

ABSTRACT:

Background

Death-Associated Protein Kinase (DAPK) is a member of the Ca2+/calmodulin regulated serine/threonine protein kinases. Its biological function has been associated with induced cell death, and in vivo use of selective small molecule inhibitors of DAPK catalytic activity has demonstrated that it is a potential therapeutic target for treatment of brain injuries and neurodegenerative diseases.

Methodology/principal findings

In the in vitro study presented here, we describe the homodimerization of DAPK catalytic domain and the crucial role played by its basic loop structure that is part of the molecular fingerprint of death protein kinases. Nanoelectrospray ionization mass spectrometry of DAPK catalytic domain and a basic loop mutant DAPK protein performed under a varie

SUBMITTER: Zimmermann M 

PROVIDER: S-EPMC2994711 | biostudies-literature | 2010 Nov

REPOSITORIES: biostudies-literature