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Structure of human dual-specificity phosphatase 27 at 2.38 angstrom resolution

  1. Author:
    Lountos, G. T.
    Tropea, J. E.
    Waugh, D. S.

  2. Author Address

    [Lountos, GT; Tropea, JE; Waugh, DS] NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21702 USA;Waugh, DS (reprint author), NCI, Macromol Crystallog Lab, Ctr Canc Res, Frederick, MD 21702 USA;waughd@mail.nih.gov
    1. Year: 2011
    2. Date: May
  2. Journal: Acta Crystallographica Section D-Biological Crystallography
    1. 67
    2. Pages: 471-479
  4. Type of Article: Article
  5. ISSN: 0907-4449
  1. Abstract:

    There are over 100 genes in the human genome that encode protein tyrosine phosphatases (PTPs) and approximately 60 of these are classified as dual-specificity phosphatases (DUSPs). Although many dual-specificity phosphatases are still not well characterized, novel functions have been discovered for some of them that have led to new insights into a variety of biological processes and the molecular basis for certain diseases. Indeed, as the functions of DUSPs continue to be elucidated, a growing number of them are emerging as potential therapeutic targets for diseases such as cancer, diabetes and inflammatory disorders. Here, the overexpression, purification and structure determination of DUSP27 at 2.38 angstrom resolution are presented.

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External Sources

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  2. DOI: 10.1107/s090744491100970x
  3. View record in Web of Science®
  4. WOS: 000290235200010

Library Notes

  1. Fiscal Year: FY2010-2011
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