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

Academic Article
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Overview

authors

  • Radhakrishnan, I.
  • PerezAlvarado, G. C.
  • Parker, D.
  • Dyson, Jane
  • Montminy, M. R.
  • Wright, Peter

publication date

  • December 1997

journal

  • Cell  Journal

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 alpha helices. The amphipathic helix alphaB of pKID interacts with a hydrophobic groove defined by helices alpha1 and alpha3 of KIX. The other pKID helix, alphaA, contacts a different face of the alpha3 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.

subject areas

  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • CREB-Binding Protein
  • Consensus Sequence
  • Cyclic AMP Response Element-Binding Protein
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Nuclear Proteins
  • Phosphopeptides
  • Protein Conformation
  • Protein Structure, Secondary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Trans-Activators
  • Transcription Factors
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Identity

International Standard Serial Number (ISSN)

  • 0092-8674

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(00)80463-8

PubMed ID

  • 9413984
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Additional Document Info

start page

  • 741

end page

  • 752

volume

  • 91

issue

  • 6

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