Crystal structure of human DUSP28.

<p>(A) DUSP28 is presented as secondary structure-labeled ribbon models, where α-helices are violet, β-strands are green, and the remaining structures are white. The serine-substituted catalytic residue is shown as a stick model and is labeled as “C103S”. (B) Stereo views of three superimposed DUSP proteins shown as C_α trace representation. Dashed circles indicate the DUSP28-specific N-terminal extension region. (C) The N-terminal region of DUSP proteins. (<i>Left</i>) N-terminal residues ahead of β1 from three DUSP proteins are presented as ribbon models and are labeled. (<i>Right</i>) Sequence alignment of N-terminal residues from DUSP28 and 10 other DUSP proteins ordered by decreasing Z-scores (noted in parenthesis). Four nonconserved proline residues in DUSP28 are labeled in red in both panels.