NMR dynamics study of the Z-DNA binding domain of human ADAR1 bound to various DNA duplexes.
Biochem Biophys Res Commun
; 428(1): 137-41, 2012 Nov 09.
Article
en En
| MEDLINE
| ID: mdl-23079620
ABSTRACT
The Z-DNA binding domain of human ADAR1 (Zα(ADAR1)) preferentially binds Z-DNA rather than B-DNA with high binding affinity. Here, we have carried out chemical shift perturbation and backbone dynamics studies of Zα(ADAR1) in the free form and in complex with three DNA duplexes, d(CGCGCG)(2), d(CACGTG)(2), and d(CGTACG)(2). This study reveals that Zα(ADAR1) initially binds to d(CGCGCG)(2) through the distinct conformation, especially in the unusually flexible ß1-loop-α2 region, from the d(CGCGCG)(2)-(Zα(ADAR1))(2) complex. This study also suggests that Zα(ADAR1) exhibits a distinct conformational change during the B-Z transition of non-CG-repeat DNA duplexes with low binding affinities compared to the CG-repeat DNA duplex.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Adenosina Desaminasa
/
ADN de Forma Z
Límite:
Humans
Idioma:
En
Revista:
Biochem Biophys Res Commun
Año:
2012
Tipo del documento:
Article