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Abstract：
The dual specificity phosphatase DUSP1 was the first mitogen activated protein kinase phosphatase (MKP) to be identified. It dephosphorylates conserved tyrosine and threonine residues in the activation loops of mitogen activated protein kinases ERK2, JNK1 and p38-alpha. Here, we report the crystal structure of the human DUSP1 catalytic domain at 2.49 Å resolution. Uniquely, the protein was crystallized as an MBP fusion protein in complex with a monobody that binds to MBP. Sulfate ions occupy the phosphotyrosine and putative phosphothreonine binding sites in the DUSP1 catalytic domain.
摘要：
双特异性磷酸酶DUSP1是第一个被鉴定的丝裂原活化蛋白激酶磷酸酶(MKP)。它使丝裂原活化蛋白激酶ERK2，JNK1和p38-alpha的活化环中保守的酪氨酸和苏氨酸残基去磷酸化。这里,我们报告了人类DUSP1催化域的晶体结构，分辨率为2.49µ。独特的,该蛋白以MBP融合蛋白的形式与结合MBP的单体形成复合物。硫酸根离子占据DUSP1催化结构域中的磷酸酪氨酸和推定的磷酸苏氨酸结合位点。
