1H, 13C and 15N backbone NMR chemical shift assignments of the C-terminal P4 domain of Ahnak.
Biomol NMR Assign
; 12(2): 253-257, 2018 10.
Article
em En
| MEDLINE
| ID: mdl-29594929
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 ß 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.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ressonância Magnética Nuclear Biomolecular
/
Proteínas de Membrana
Idioma:
En
Revista:
Biomol NMR Assign
Assunto da revista:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Ano de publicação:
2018
Tipo de documento:
Article
País de afiliação:
Austrália