Biomolecular NMR Assignments

, Volume 12, Issue 2, pp 253–257 | Cite as

1H, 13C and 15N backbone NMR chemical shift assignments of the C-terminal P4 domain of Ahnak

  • Srinivasan Sundararaj
  • Dmitry Shishmarev
  • Yiechang Lin
  • Shouvik Aditya
  • Marco G. Casarotto


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.


Ahnak NMR Resonance assignments Circular dichroism Chemical shift index CaV1.2 modulation 



This work was supported by Grant APP1126201 from the Australian National Health and Medical Research Council (NHMRC) to MGC. The study made use of the NMR facility at the Research School of Chemistry at the Australian National University. The authors would like to thank Ms Elmira Bahraminejad for help with the circular dichroism spectroscopy.

Compliance with ethical standards

Conflict of interest

The authors declare no conflict of interest.


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© Springer Science+Business Media B.V., part of Springer Nature 2018

Authors and Affiliations

  1. 1.ACRF Department of Cancer Biology and Therapeutics, The John Curtin School of Medical ResearchThe Australian National UniversityCanberraAustralia

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