Serine/threonine-protein phosphatase 2A activator (PPP2R4) has been classified as a subunit of serine/threonine-protein phosphatase (PP2A). It has three subdomains- a core, a lid and a linker.
Synonyms: Anti-PPP2R4; Anti-PR53; Anti-PP2A, subunit B', PR53 isoform; Anti-PTPA; Anti-Phosphotyrosyl phosphatase activator; Anti-Serine/threonine-protein phosphatase 2A regulatory subunit B’
Storage: -20C
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Biochem Physiol Actions: Serine/threonine-protein phosphatase 2A activator (PPP2R4) fastens the folding of proteins and also catalyzes the cis-trans isomerization of peptide bonds in oligopeptides. It functions as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A). By inducing a conformational change in the catalytic subunit, it modulates its activity and substrate specificity. Structural analysis depicts a highly conserved surface patch, which borders the three subdomains, and an associated deep pocket located between the core and the linker subdomains. Both of these are responsible for binding to PP2A and ATP. In presence of ATP and Mg2+, PPP2R4 reactivates the inactive phosphatase PP2A-phosphatase methylesterase complexes. The PP2A(D):PPP2R4 complex has an ATPase activity, which influences the phosphotyrosyl phosphatase activity.
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