Mutational analysis of the KIX domain of CBP reveals residues critical for SREBP binding |
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Authors: | Liu Ya-Ping Chang Ching-Wen Chang Kung-Yao |
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Affiliation: | Institute of Biochemistry, National Chung-Hsing University, 250 Kuo-Kung Road, Taichung 402, Taiwan. |
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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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Keywords: | Sterol-responsive element binding protein cAMP-responsive element binding protein CREB binding protein Structure-based mutagenesis Protein-protein interaction Post-translational modification |
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