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

doi:10.1007/s12104-018-9818-3

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

Biomol NMR Assign. 2018 Oct;12(2):253-257. doi: 10.1007/s12104-018-9818-3. Epub 2018 Mar 28.

Authors

Srinivasan Sundararaj¹, Dmitry Shishmarev², Yiechang Lin¹, Shouvik Aditya¹, Marco G Casarotto³

Affiliations

¹ ACRF Department of Cancer Biology and Therapeutics, The John Curtin School of Medical Research, The Australian National University, Canberra, ACT, 2601, Australia.
² ACRF Department of Cancer Biology and Therapeutics, The John Curtin School of Medical Research, The Australian National University, Canberra, ACT, 2601, Australia. dmitry.shishmarev@anu.edu.au.
³ ACRF Department of Cancer Biology and Therapeutics, The John Curtin School of Medical Research, The Australian National University, Canberra, ACT, 2601, Australia. marco.casarotto@anu.edu.au.

PMID: 29594929
DOI: 10.1007/s12104-018-9818-3

Abstract

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 (Ca_V1.2). 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 Ca_V1.2-Ahnak complex.

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

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Binding Sites
Calcium Channels, L-Type / metabolism
Membrane Proteins / chemistry*
Membrane Proteins / metabolism
Nuclear Magnetic Resonance, Biomolecular*
Protein Domains
Protein Subunits / chemistry
Protein Subunits / metabolism

Substances

Calcium Channels, L-Type
L-type calcium channel alpha(1C)
Membrane Proteins
Protein Subunits