Crystal structure of the human dual specificity phosphatase 1 catalytic domain
| Autor: | Joseph E. Tropea, Rajesh Gumpena, George T. Lountos, Scott Cherry, Sreejith Raran-Kurussi, David S. Waugh |
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| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Phosphothreonine binding biology Phosphatase DUSP6 Protein phosphatase 2 Biochemistry Monobody 03 medical and health sciences Maltose-binding protein 030104 developmental biology 0302 clinical medicine 030220 oncology & carcinogenesis Mitogen-activated protein kinase Dual-specificity phosphatase biology.protein Molecular Biology |
| Zdroj: | Protein Science. 27:561-567 |
| ISSN: | 0961-8368 |
| DOI: | 10.1002/pro.3328 |
| Popis: | 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 A 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. |
| Databáze: | OpenAIRE |
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