Open AccessStructure of human dual‐specificity phosphatase 27 at 2.38 Å resolution
Author(s) -
Lountos George T.,
Tropea Joseph E.,
Waugh David S.
Publication year - 2011
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s090744491100970x
Subject(s) - dual specificity phosphatase , protein tyrosine phosphatase , phosphatase , computational biology , biology , dual (grammatical number) , gene , encode , tyrosine , biochemistry , phosphorylation , art , literature
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 Å resolution are presented.