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Crystal structure of the human dual specificity phosphatase 1 catalytic domain

  1. Author:
    Gumpena, Rajesh
    Lountos, George
    Raran-Kurussi, Sreejith
    Tropea, Joseph
    Cherry, Scott
    Waugh, David

  2. Author Address

    Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD 21702., Basic Science Program, Leidos Biomedical Research, Inc., Frederick National Laboratory for Cancer Research, Frederick, MD 21702., TIFR Centre for Interdisciplinary Sciences, Hyderabad-500075, India.,
    1. Year: 2018
    2. Date: Feb
    3. Epub Date: 2017 10 20
  2. Journal: Protein science : a publication of the Protein Society
    1. 27
    2. 2
    3. Pages: 561-567
  4. Type of Article: Article
  5. ISSN: 0961-8368
  1. 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. This article is protected by copyright. All rights reserved. © 2017 The Protein Society.

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External Sources

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  2. DOI: 10.1002/pro.3328
  3. PMID: 29052270
  4. View record in Web of Science®
  5. WOS: 000422956600018

Library Notes

  1. Fiscal Year: FY2017-2018
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