Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions

Ishwar Radhakrishnan, Gabriela C. Pérez-Alvarado, David Parker, H. Jane Dyson, Marc R. Montminy, Peter E. Wright*

*Corresponding author for this work

Research output: Contribution to journalArticle

571 Scopus citations

Abstract

The nuclear factor CREB activates transcription of target genes in part through direct interactions with the KIX domain of the coactivator CBP in a phosphorylation-dependent manner. The solution structure of the complex formed by the phosphorylated kinase-inducible domain (pKID) of CREB with KIX reveals that pKID undergoes a coil → helix folding transition upon binding to KIX, forming two α helices. The amphipathic helix αB of pKID interacts with a hydrophobic groove defined by helices αl and α3 of KIX. The other pKID helix, αA, contacts a different face of the α3 helix. The phosphate group of the critical phosphoserine residue of pKID forms a hydrogen bond to the side chain of Tyr-658 of KIX. The structure provides a model for interactions between other transactivation domains and their targets.

Original languageEnglish (US)
Pages (from-to)741-752
Number of pages12
JournalCell
Volume91
Issue number6
DOIs
StatePublished - Dec 12 1997

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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