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Mutational analysis of the KIX domain of CBP reveals residues critical for SREBP binding
Author(s) -
Liu Ya-Ping,
Chang Ching-Wen,
Chang Kung-Yao
Publication year - 2003
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(03)01200-6
Subject(s) - biophysics , mutagenesis , helix (gastropod) , binding site , chemistry , creb binding protein , plasma protein binding , biochemistry , biology , mutation , creb , transcription factor , gene , ecology , snail
Structure‐based mutagenesis was used to probe the binding surface for the activation domain of sterol‐responsive element binding protein (SREBP) in the KIX domain of CREB binding protein. A set of conserved residues scattering in the α2 helix and the extended C‐terminal region of α3 helix in the KIX domain including two arginines previously characterized as a hot spot for cofactor‐mediated methylation was shown to be crucial for SREBP–KIX interaction, and was not essential for phosphorylated KID recognition. Therefore, our results suggest the existence of a SREBP binding site formed by positively charged residues in the C‐terminal part of the extended α3 helix of the KIX domain distinct from the previously identified phosphorylated KID binding site.