Mutational analysis of the KIX domain of CBP reveals residues critical for SREBP binding
- PMID: 14623102
- DOI: 10.1016/s0014-5793(03)01200-6
Mutational analysis of the KIX domain of CBP reveals residues critical for SREBP binding
Abstract
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 alpha2 helix and the extended C-terminal region of alpha 3 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 alpha 3 helix of the KIX domain distinct from the previously identified phosphorylated KID binding site.
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