SH2-directed ligands of the Lck tyrosine kinase.
J Med Chem
; 43(6): 1173-9, 2000 Mar 23.
Article
em En
| MEDLINE
| ID: mdl-10737750
ABSTRACT
Two separate libraries, prepared via parallel synthesis, were employed to identify low-molecular-weight SH2-targeted ligands for the Lck tyrosine protein kinase. These libraries were constructed to furnish non-amino acid analogues of the (1) Glu-Glu and (2) Ile residues of the Lck SH2 domain peptide ligand Ac-pTyr-Glu-Glu-Ile-amide. The lead compound acquired in this study exhibits a dissociation constant for the Lck SH2 domain that is comparable to that displayed by Ac-pTyr-Glu-Glu-Ile-amide. These results demonstrate that the standard amino acid residues Glu-Glu-Ile can be completely replaced with non-amino acid moieties without loss of SH2 affinity.
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Base de dados:
MEDLINE
Assunto principal:
Tirosina
/
Domínios de Homologia de src
/
Proteína Tirosina Quinase p56(lck) Linfócito-Específica
/
Cumarínicos
/
Amidas
Idioma:
En
Revista:
J Med Chem
Assunto da revista:
QUIMICA
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Estados Unidos