Structure-based design, synthesis, and X-ray crystallography of a high-affinity antagonist of the Grb2-SH2 domain containing an asparagine mimetic.
J Med Chem
; 42(13): 2358-63, 1999 Jul 01.
Article
em En
| MEDLINE
| ID: mdl-10395476
ABSTRACT
Previous efforts in the search for molecules capable of blocking the associations between the activated tyrosine kinase growth factor receptors and the SH2 domain of Grb2 had resulted in the identification of 3-amino-Z-pTyr-Ac6c-Asn-NH2, a high-affinity and selective antagonist of this SH2 domain. In the present paper, we report the successful replacement of asparagine in this compound by a beta-amino acid mimetic, which brings us closer to our objective of identifying a Grb2-SH2 antagonist suitable for pharmacological investigations.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Asparagina
/
Tirosina
/
Proteínas de Transporte
/
Domínios de Homologia de src
/
Cicloexanos
/
Proteínas Adaptadoras de Transdução de Sinal
Tipo de estudo:
Prognostic_studies
Idioma:
En
Ano de publicação:
1999
Tipo de documento:
Article