Role of amino acid residues surrounding the phosphorylation site in peptide substrates of G protein-coupled receptor kinase 2 (GRK2).
Amino Acids
; 48(12): 2875-2880, 2016 12.
Article
em En
| MEDLINE
| ID: mdl-27714516
ABSTRACT
A series of amino acid substitutions was made in a previously identified ß-tubulin-derived GRK2 substrate peptide (404DEMEFTEAESNMN416) to examine the role of amino acid residues surrounding the phosphorylation site. Anionic amino acid residues surrounding the phosphorylation site played an important role in the affinity for GRK2. Compared to the original peptide, a modified peptide (Ac-EEMEFSEAEANMN-NH2) exhibited markedly higher affinity for GRK2, but very low affinity for GRK5, suggesting that it can be a sensitive and selective peptide for GRK2.
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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
/
Tubulina (Proteína)
/
Substituição de Aminoácidos
/
Quinase 2 de Receptor Acoplado a Proteína G
Limite:
Humans
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article