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Crystal structure of the human dual specificity phosphatase 1 catalytic domain.

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.

SUBMITTER: Gumpena R

PROVIDER: S-EPMC5775162 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

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Crystal structure of the human dual specificity phosphatase 1 catalytic domain.

Gumpena Rajesh R Lountos George T GT Raran-Kurussi Sreejith S Tropea Joseph E JE Cherry Scott S Waugh David S DS

Protein science : a publication of the Protein Society 20171121 2

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 ...[more]

PMID: 29052270

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