Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1.

摘要: The crystal structure of mammalian protein phosphatase-1, complexed with the toxin microcystin and determined at 2.1 A resolution, reveals that it is a metalloenzyme unrelated in architecture to tyrosine phosphatases. Two metal ions are positioned by central beta-alpha-beta-alpha-beta scaffold active site, from which emanate three surface grooves potential binding sites for substrates inhibitors. carboxy terminus end one such regulatory sequences following domain might modulate function. fold catalytic expected be closely preserved phosphatases 2A 2B (calcineurin).