Utilization of a nitrogen-sulfur nonbonding interaction in the design of new 2-aminothiazol-5-yl-pyrimidines as p38α MAP kinase inhibitors.
Bioorg Med Chem Lett
; 20(19): 5864-8, 2010 Oct 01.
Article
em En
| MEDLINE
| ID: mdl-20732813
ABSTRACT
The design, synthesis, and structure-activity relationships (SAR) of a series of 2-aminothiazol-5-yl-pyrimidines as novel p38α MAP kinase inhibitors are described. These efforts led to the identification of 41 as a potent p38α inhibitor that utilizes a unique nitrogen-sulfur intramolecular nonbonding interaction to stabilize the conformation required for binding to the p38α active site. X-ray crystallographic studies that confirm the proposed binding mode of this class of inhibitors in p38 α and provide evidence for the proposed intramolecular nitrogen-sulfur interaction are discussed.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Pirimidinas
/
Enxofre
/
Tiazóis
/
Proteína Quinase 14 Ativada por Mitógeno
/
Inibidores de Proteínas Quinases
/
Nitrogênio
Idioma:
En
Revista:
Bioorg Med Chem Lett
Ano de publicação:
2010
Tipo de documento:
Article