The structural basis for control of eukaryotic protein kinases.
Annu Rev Biochem
; 81: 587-613, 2012.
Article
en En
| MEDLINE
| ID: mdl-22482904
ABSTRACT
Eukaryotic protein kinases are key regulators of cell processes. Comparison of the structures of protein kinase domains, both alone and in complexes, allows generalizations to be made about the mechanisms that regulate protein kinase activation. Protein kinases in the active state adopt a catalytically competent conformation upon binding of both the ATP and peptide substrates that has led to an understanding of the catalytic mechanism. Docking sites remote from the catalytic site are a key feature of several substrate recognition complexes. Mechanisms for kinase activation through phosphorylation, additional domains or subunits, by scaffolding proteins and by kinase dimerization are discussed.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Proteínas Quinasas
/
Dominio Catalítico
/
Eucariontes
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Annu Rev Biochem
Año:
2012
Tipo del documento:
Article
País de afiliación:
Reino Unido