Ahnak is a ~ 700 kDa polypeptide that was originally identified as a tumour-related nuclear phosphoprotein, but later recognized to play a variety of diverse physiological roles related to cell architecture and migration. A critical function of Ahnak is modulation of Ca2+ signaling in cardiomyocytes by interacting with the β subunit of the L-type Ca2+ channel (CaV1.2). Previous studies have identified the C-terminal region of Ahnak, designated as P3 and P4 domains, as a key mediator of its functional activity. We report here the nearly complete 1H, 13C and 15N backbone NMR chemical shift assignments of the 11 kDa C-terminal P4 domain of Ahnak. This study lays the foundations for future investigations of functional dynamics, structure determination and interaction site mapping of the CaV1.2-Ahnak complex.
CITATION STYLE
Sundararaj, S., Shishmarev, D., Lin, Y., Aditya, S., & Casarotto, M. G. (2018). 1H, 13C and 15N backbone NMR chemical shift assignments of the C-terminal P4 domain of Ahnak. Biomolecular NMR Assignments, 12(2), 253–257. https://doi.org/10.1007/s12104-018-9818-3
Mendeley helps you to discover research relevant for your work.