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Protein Sci. 2018 Feb;27(2):561-567. doi: 10.1002/pro.3328. Epub 2017 Nov 21.

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

Author information

1
Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD, 21702.
2
Frederick National Laboratory for Cancer Research, Basic Science Program, Leidos Biomedical Research, Inc, Frederick, 21702, MD.
3
TIFR Centre for Interdisciplinary Sciences, Hyderabad, 500075, India.

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.

KEYWORDS:

DUSP; crystallization chaperone; dual specificity phosphatase; maltose-binding protein; monobody; sulfate ions

PMID:
29052270
PMCID:
PMC5775162
DOI:
10.1002/pro.3328
[Indexed for MEDLINE]
Free PMC Article

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