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Crystal structure of the human dual specificity phosphatase 1 catalytic domain
Author(s) -
Gumpena Rajesh,
Lountos George T.,
RaranKurussi Sreejith,
Tropea Joseph E.,
Cherry Scott,
Waugh David S.
Publication year - 2018
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1002/pro.3328
Subject(s) - dual specificity phosphatase , phosphatase , dusp6 , protein tyrosine phosphatase , threonine , protein kinase a , biochemistry , chemistry , c raf , kinase , fusion protein , phosphorylation , biology , microbiology and biotechnology , protein phosphatase 2 , mitogen activated protein kinase kinase , serine , recombinant dna , gene
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.