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The crystal structure of a human PP2A phosphatase activator reveals a novel fold and highly conserved cleft implicated in protein-protein interactions
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
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2006 In: Journal of Biological Chemistry, ISSN 0021-9258, Vol. 281, 22434-22438 p.Article in journal (Refereed) Published
Place, publisher, year, edition, pages
2006. Vol. 281, 22434-22438 p.
URN: urn:nbn:se:su:diva-25543OAI: diva2:199930
Part of urn:nbn:se:su:diva-8261Available from: 2008-10-23 Created: 2008-10-14Bibliographically approved
In thesis
1. Structural Studies on PP2A and Methods in Protein Production
Open this publication in new window or tab >>Structural Studies on PP2A and Methods in Protein Production
2008 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

PP2A is a major phosphatase in the cell that participates in multiple cell signaling pathways. It is a heterotrimer of a core dimer and variable regulatory subunits. Details of its structure, function and regulation are slowly emerging. Here, the structure of two regulators of PP2A are de-scribed; PTPA and B56γ. PTPA is a highly conserved enzyme that plays a crucial role in PP2A activity but whose biochemical function is still unclear. B56γ is a PP2A regulatory subunit linked to cancer and the structure presented here of B56γ in its free form is particularly valuable in light of the recent structures of the PP2A holoenzyme and core dimer.

Protein production is a major bottleneck in structural genomic projects. Here, we describe two novel methods for improved protein production. The first is a colony based screening method where any DNA library can be screened for soluble expression of recombinant proteins in E.coli. The second method involves improvements of the well established IMAC purification method. We have seen that a low molecular weight component of E.coli lysate decreases the binding capacity of IMAC columns and by removing the low molecular weight components, recombinant proteins only present at low levels in E.coli lysate can be purified, which has previously been believed to be unfeasible.

Place, publisher, year, edition, pages
Stockholm: Institutionen för biokemi och biofysik, 2008. 53 p.
PP2A, PTPA, B56γ, Protein Production
National Category
Structural Biology
Research subject
urn:nbn:se:su:diva-8261 (URN)978-91-7155-750 (ISBN)
Public defence
2008-11-14, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 12 A, Stockholm, 10:00
Available from: 2008-10-23 Created: 2008-10-14Bibliographically approved

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