Abstract
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 the tyrosine phosphatases. Two metal ions are positioned by a central beta-alpha-beta-alpha-beta scaffold at the active site, from which emanate three surface grooves that are potential binding sites for substrates and inhibitors. The carboxy terminus is positioned at the end of one of the grooves such that regulatory sequences following the domain might modulate function. The fold of the catalytic domain is expected to be closely preserved in protein phosphatases 2A and 2B (calcineurin).
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Binding Sites
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Catalysis
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Crystallography, X-Ray
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Dopamine and cAMP-Regulated Phosphoprotein 32
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Escherichia coli
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Humans
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Intracellular Signaling Peptides and Proteins
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Metals / chemistry
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Microcystins
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Models, Molecular
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Molecular Sequence Data
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Nerve Tissue Proteins / chemistry
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Nuclear Proteins
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Peptides, Cyclic / chemistry
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Phosphoprotein Phosphatases / antagonists & inhibitors
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Phosphoprotein Phosphatases / chemistry*
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Phosphoproteins*
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Protein Conformation
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Protein Phosphatase 1
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Proteins / chemistry
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RNA-Binding Proteins
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Rabbits
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Recombinant Proteins / chemistry
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Sequence Homology, Amino Acid
Substances
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ANP32A protein, human
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Dopamine and cAMP-Regulated Phosphoprotein 32
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Intracellular Signaling Peptides and Proteins
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Metals
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Microcystins
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Nerve Tissue Proteins
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Nuclear Proteins
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Peptides, Cyclic
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Phosphoproteins
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Proteins
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RNA-Binding Proteins
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Recombinant Proteins
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microcystin
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Phosphoprotein Phosphatases
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Protein Phosphatase 1