Dynamic Response of the C2 Domain of Protein Kinase Cα to Ca2+ Binding.
Biophys J
; 111(8): 1655-1667, 2016 Oct 18.
Article
in En
| MEDLINE
| ID: mdl-27760353
ABSTRACT
Ca2+-dependent conserved-region 2 (C2) domains target their host signaling proteins to anionic membranes. The Ca2+-binding event is a prerequisite for membrane association. Here, we investigate multiscale metal-ion-dependent dynamics of the C2 domain of protein kinase Cα (C2α) using NMR spectroscopy. Interactions with metal ions attenuate microsecond-timescale motions of the loop regions, indicating that preorganization of the metal-binding loops occurs before membrane insertion. Binding of a full complement of Ca2+ ions has a profound effect on the millisecond-timescale dynamics of the N- and C-terminal regions of C2α. We propose that Ca2+ binding allosterically destabilizes the terminal regions of C2α and thereby facilitates the conformational rearrangement necessary for full membrane insertion and activation of protein kinase Cα.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Calcium
/
Protein Kinase C-alpha
Type of study:
Prognostic_studies
Language:
En
Journal:
Biophys J
Year:
2016
Type:
Article