2y96
From Proteopedia
Structure of human dual-specificity phosphatase 27
Structural highlights
FunctionDUS29_HUMAN Dual specificity phosphatase able to dephosphorylate phosphotyrosine, phosphoserine and phosphothreonine residues within the same substrate, with a preference for phosphotyrosine as a substrate (PubMed:17498703). Involved in the modulation of intracellular signaling cascades. In skeletal muscle regulates systemic glucose homeostasis by activating, AMPK, an energy sensor protein kinase (By similarity). Affects MAP kinase signaling though modulation of the MAPK1/2 cascade in skeletal muscle promoting muscle cell differentiation, development and atrophy (By similarity).[UniProtKB:Q8BK84][1] Publication Abstract from PubMedThere 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 A resolution are presented. Structure of human dual-specificity phosphatase 27 at 2.38 A resolution.,Lountos GT, Tropea JE, Waugh DS Acta Crystallogr D Biol Crystallogr. 2011 May;67(Pt 5):471-9. Epub 2011, Apr 16. PMID:21543850[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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