title: Structure of human dual-specificity phosphatase 27 at 2.38 Å resolution.
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 Å resolution are presented.
authors.affiliation: Macromolecular Crystallography Laboratory, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD 21702, USA.
authors.forename: George T
authors.initials: GT
authors.lastname: Lountos
authors.forename: Joseph E
authors.initials: JE
authors.lastname: Tropea
authors.forename: David S
authors.initials: DS
authors.lastname: Waugh
mesh_terms: D020134:Catalytic Domain; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D010749:Phosphoprotein Phosphatases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D040681:Structural Homology, Protein; D015854:Up-Regulation
chemical_list: D010749:Phosphoprotein Phosphatases; C522887:STYXL2 protein, human