Figure 1
Comparison of CEBP proteins. (A) Multiple amino acid alignment of CEBP proteins. Five members of the CEBP gene family were profiled by the ClustalX program (http://bips.u-strasbg.fr/fr/Documentation/ClustalX). Basic DNA-binding and leucine zipper motifs that compose the bZIP domain are colored blue and red, respectively. A proline- or glycine-rich region suggesting transactivating domains are shown in green. *Positions that have a single, fully conserved residue; a colon indicates strong homology, and a period indicates weak homology, respectively based on the Gonnet Pam250 matrix. (B) Schematic diagram of CEBP structures and mutation sites. Basic DNA-binding motif, leucine zipper motif, and potential transactivating domain are shown in blue, red, and green, respectively. The ATG start codons, including potential initiation codons, are indicated by the arrows with the amino acid numbering. The protein sizes are shown on the right side. Arrowheads indicate the positions of mutations detected in this study.

Comparison of CEBP proteins. (A) Multiple amino acid alignment of CEBP proteins. Five members of the CEBP gene family were profiled by the ClustalX program (http://bips.u-strasbg.fr/fr/Documentation/ClustalX). Basic DNA-binding and leucine zipper motifs that compose the bZIP domain are colored blue and red, respectively. A proline- or glycine-rich region suggesting transactivating domains are shown in green. *Positions that have a single, fully conserved residue; a colon indicates strong homology, and a period indicates weak homology, respectively based on the Gonnet Pam250 matrix. (B) Schematic diagram of CEBP structures and mutation sites. Basic DNA-binding motif, leucine zipper motif, and potential transactivating domain are shown in blue, red, and green, respectively. The ATG start codons, including potential initiation codons, are indicated by the arrows with the amino acid numbering. The protein sizes are shown on the right side. Arrowheads indicate the positions of mutations detected in this study.

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