Met-204 and Tyr-205 are together important for binding GLP-1 receptor agonists but not their N-terminally truncated analogues.
Protein Pept Lett
; 11(1): 15-22, 2004 Feb.
Article
em En
| MEDLINE
| ID: mdl-14965274
ABSTRACT
A mutagenesis study to systematically analyse residues spanning the first extracellular loop of the GLP-1 receptor identified a double mutant, Met-204/Tyr-205-Ala/Ala, which displayed markedly reduced affinity for the natural agonist GLP-1; slightly reduced affinity for its analogue exendin-4; and unaltered affinity for several N-terminally truncated analogues of GLP-1 and exendin-4. This suggests that the locus is important for the formation of the binding site for the N-terminal residues of peptide agonists.
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Base de dados:
MEDLINE
Assunto principal:
Fragmentos de Peptídeos
/
Peptídeos
/
Precursores de Proteínas
/
Tirosina
/
Peçonhas
/
Glucagon
/
Receptores de Glucagon
/
Metionina
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Protein Pept Lett
Assunto da revista:
BIOQUIMICA
Ano de publicação:
2004
Tipo de documento:
Article
País de afiliação:
Reino Unido