Open AccessOverproduction, purification and structure determination of human dual‐specificity phosphatase 14
Author(s) -
Lountos George T.,
Tropea Joseph E.,
Cherry Scott,
Waugh David S.
Publication year - 2009
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
ISSN - 1399-0047
DOI - 10.1107/s0907444909023762
Subject(s) - dual specificity phosphatase , protein tyrosine phosphatase , phosphatase , kinase , serine , microbiology and biotechnology , dusp6 , mapk/erk pathway , mitogen activated protein kinase , phosphorylation , biology , biochemistry , protein phosphatase 2
Dual‐specificity phosphatases (DUSPs) are enzymes that participate in the regulation of biological processes such as cell growth, differentiation, transcription and metabolism. A number of DUSPs are able to dephosphorylate phosphorylated serine, threonine and tyrosine residues on mitogen‐activated protein kinases (MAPKs) and thus are also classified as MAPK phosphatases (MKPs). As an increasing number of DUSPs are being identified and characterized, there is a growing need to understand their biological activities at the molecular level. There is also significant interest in identifying DUSPs that could be potential targets for drugs that modulate MAPK‐dependent signaling and immune responses, which have been implicated in a variety of maladies including cancer, infectious diseases and inflammatory disorders. Here, the overproduction, purification and crystal structure at 1.88 Å resolution of human dual‐specificity phosphatase 14, DUSP14 (MKP6), are reported. This structural information should accelerate the study of DUSP14 at the molecular level and may also accelerate the discovery and development of novel therapeutic agents.