2ixn: Difference between revisions

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[[Image:2ixn.gif|left|200px]]
{{Seed}}
[[Image:2ixn.png|left|200px]]


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{{STRUCTURE_2ixn|  PDB=2ixn  |  SCENE=  }}  
{{STRUCTURE_2ixn|  PDB=2ixn  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR YPA2 PTPA2'''
===CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR YPA2 PTPA2===




==Overview==
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PTPA, an essential and specific activator of protein phosphatase 2A (PP2A), functions as a peptidyl prolyl isomerase (PPIase). We present here the crystal structures of human PTPA and of the two yeast orthologs (Ypa1 and Ypa2), revealing an all alpha-helical protein fold that is radically different from other PPIases. The protein is organized into two domains separated by a groove lined by highly conserved residues. To understand the molecular mechanism of PTPA activity, Ypa1 was cocrystallized with a proline-containing PPIase peptide substrate. In the complex, the peptide binds at the interface of a peptide-induced dimer interface. Conserved residues of the interdomain groove contribute to the peptide binding site and dimer interface. Structure-guided mutational studies showed that in vivo PTPA activity is influenced by mutations on the surface of the peptide binding pocket, the same mutations that also influenced the in vitro activation of PP2Ai and PPIase activity.
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==About this Structure==
==About this Structure==
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[[Category: Isomerase]]
[[Category: Isomerase]]
[[Category: Pp2a phosphatase activator prolyl isomerase ptpa]]
[[Category: Pp2a phosphatase activator prolyl isomerase ptpa]]
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Revision as of 07:27, 28 July 2008

File:2ixn.png

Template:STRUCTURE 2ixn

CRYSTAL STRUCTURE OF THE PP2A PHOSPHATASE ACTIVATOR YPA2 PTPA2

Template:ABSTRACT PUBMED 16885030

About this Structure

2IXN is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity., Leulliot N, Vicentini G, Jordens J, Quevillon-Cheruel S, Schiltz M, Barford D, van Tilbeurgh H, Goris J, Mol Cell. 2006 Aug 4;23(3):413-24. PMID:16885030

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