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Conformational preferences in the Ser 133 ‐phosphorylated and non‐phosphorylated forms of the kinase inducible transactivation domain of CREB
Author(s) -
Radhakrishnan Ishwar,
Pérez-Alvarado Gabriela C,
Dyson H.Jane,
Wright Peter E
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00680-2
Subject(s) - transactivation , phosphorylation , coactivator , creb , chemistry , heteronuclear molecule , biophysics , folding (dsp implementation) , creb binding protein , transcription factor , biochemistry , nuclear magnetic resonance spectroscopy , biology , stereochemistry , gene , electrical engineering , engineering
Phosphorylation of Ser 133 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 Ser 133 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.