Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation.
Cell
; 77(3): 451-9, 1994 May 06.
Article
en En
| MEDLINE
| ID: mdl-8181063
The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA complex has been solved and refined at 2.8 A resolution. This structure proves that bHLH and bHLH-leucine zipper (bHLH-ZIP) proteins are remarkably similar; it helps us understand subtle differences in binding preferences for these proteins; and it has surprising implications for our understanding of transcription. Specifically, Ala-114 and Thr-115, which are required for positive control in the myogenic proteins, are buried at the protein-DNA interface. These residues are not available for direct protein-protein contacts, but they may determine the conformation of Arg-111. Comparisons with Max suggest that the conformation of this arginine, which is different in the two structures, may play an important role in myogenic transcription.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Polinucleótidos
/
Conformación Proteica
/
Factores de Transcripción
/
Proteína MioD
/
Secuencias Hélice-Asa-Hélice
Tipo de estudio:
Prognostic_studies
Idioma:
En
Revista:
Cell
Año:
1994
Tipo del documento:
Article
Pais de publicación:
Estados Unidos