Assembly of allosteric macromolecular switches: lessons from PKA.
Nat Rev Mol Cell Biol
; 13(10): 646-58, 2012 Oct.
Article
en En
| MEDLINE
| ID: mdl-22992589
ABSTRACT
Protein kinases are dynamic molecular switches that have evolved to be only transiently activated. Kinase activity is embedded within a conserved kinase core, which is typically regulated by associated domains, linkers and interacting proteins. Moreover, protein kinases are often tethered to large macromolecular complexes to provide tighter spatiotemporal control. Thus, structural characterization of kinase domains alone is insufficient to explain protein kinase function and regulation in vivo. Recent progress in structural characterization of cyclic AMP-dependent protein kinase (PKA) exemplifies how our knowledge of kinase signalling has evolved by shifting the focus of structural studies from single kinase subunits to macromolecular complexes.
Texto completo:
1
Base de datos:
MEDLINE
Asunto principal:
Proteínas Quinasas Dependientes de AMP Cíclico
/
Sustancias Macromoleculares
Idioma:
En
Revista:
Nat Rev Mol Cell Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
Año:
2012
Tipo del documento:
Article