Conformational preferences in the Ser133-phosphorylated and non- phosphorylated forms of the kinase inducible transactivation domain of CREB

Ishwar Radhakrishnan, Gabriela C. Pérez-Alvarado, H. Jane Dyson, Peter E. Wright*

*Corresponding author for this work

Research output: Contribution to journalArticle

122 Scopus citations

Abstract

Phosphorylation of Ser133 within the kinase inducible transactivation domain (KID) of the transcription factor CREB potentiates interaction with the KIX domain of coactivator CBP. Heteronuclear NMR spectroscopic analyses reveal that the KID domain is largely unstructured except for residues that comprise the αA helix in the pKID-KIX complex, which populate helical conformations to a significant extent (>50%). The helical content in the αB region is very small in the non-phosphorylated form (~ 10%) although a small increase is detected upon Ser133 phosphorylation. The intrinsic bias towards helical conformations probably facilitates folding of the KID domain upon binding to KIX while the principal role of the phosphate group appears to be largely in mediating the intermolecular interactions in the pKID-KIX complex.

Original languageEnglish (US)
Pages (from-to)317-322
Number of pages6
JournalFEBS Letters
Volume430
Issue number3
DOIs
StatePublished - Jul 3 1998

Keywords

  • Conformational change
  • Nuclear magnetic resonance spectroscopy
  • Protein phosphorylation
  • Protein-protein interaction
  • Transactivation domain structure
  • Transcription activation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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