Structural insights into interactions of C/EBP transcriptional activators with the Taz2 domain of p300.
Acta Crystallogr D Biol Crystallogr
; 70(Pt 7): 1914-21, 2014 Jul.
Article
em En
| MEDLINE
| ID: mdl-25004968
ABSTRACT
Members of the C/EBP family of transcription factors bind to the Taz2 domain of p300/CBP and mediate its phosphorylation through the recruitment of specific kinases. Short sequence motifs termed homology boxes A and B, which comprise their minimal transactivation domains (TADs), are conserved between C/EBP activators and are necessary for specific p300/CBP binding. A possible mode of interaction between C/EBP TADs and the p300 Taz2 domain was implied by the crystal structure of a chimeric protein composed of residues 1723-1818 of p300 Taz2 and residues 37-61 of C/EBPâ. The segment corresponding to the C/EBPâ TAD forms two orthogonally disposed helices connected by a short linker and interacts with the core structure of Taz2 from a symmetry-related molecule. It is proposed that other members of the C/EBP family interact with the Taz2 domain in the same manner. The position of the C/EBPâ peptide on the Taz2 protein interaction surface suggests that the N-termini of C/EBP proteins are unbound in the C/EBP-p300 Taz2 complex. This observation is in agreement with the known location of the docking site of protein kinase HIPK2 in the C/EBPß N-terminus, which associates with the C/EBPß-p300 complex.
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Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas Estimuladoras de Ligação a CCAAT
/
Fatores de Transcrição de p300-CBP
Idioma:
En
Revista:
Acta Crystallogr D Biol Crystallogr
Ano de publicação:
2014
Tipo de documento:
Article
País de afiliação:
Estados Unidos