Backbone and side chain resonance assignments of the C-terminal domain of human TGIF1.
Biomol NMR Assign
; 13(2): 357-360, 2019 10.
Article
en En
| MEDLINE
| ID: mdl-31388821
ABSTRACT
TGIF1 is an essential regulator of cell differentiation in various biological processes, and is associated with holoprosencephaly and many cancers. The C-terminal domain of TGIF1 that was originally defined as repressive domain 2 can interact with a variety of proteins, such as transcription factor Smad2 and co-repressor Sin3A, to mediate the regulative roles of TGIF1 in diverse cell signaling pathways. However, the recognition mechanism of TGIF1 C-terminal domain for different interacting proteins remains unknown. Here, we report the nearly complete 1H, 13C, and 15N backbone and side chain resonance assignments of TGIF1 C-terminal domain (residues 256-375), laying a foundation for further research on the structure-function relationship of TGIF1.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Proteínas Represoras
/
Proteínas de Homeodominio
/
Resonancia Magnética Nuclear Biomolecular
Límite:
Humans
Idioma:
En
Revista:
Biomol NMR Assign
Asunto de la revista:
BIOLOGIA MOLECULAR
/
MEDICINA NUCLEAR
Año:
2019
Tipo del documento:
Article
País de afiliación:
China