Abstract
We have proposed computer-generated models of the catalytic subunits of the serine-threonine protein phosphatases PP1 and PP2A complexed with their endogenous substrate phospho-DARPP-32, and several known naturally occurring inhibitors. This study is part of an overall effort to elucidate the signal transduction pathways in which PP1 and PP2A may play an important role.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Amino Acid Sequence
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Enzyme Inhibitors / chemistry*
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Enzyme Inhibitors / metabolism
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Enzyme Inhibitors / pharmacology
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Models, Molecular
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Molecular Sequence Data
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Okadaic Acid / chemistry*
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Okadaic Acid / metabolism
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Okadaic Acid / pharmacology
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Phosphoprotein Phosphatases / antagonists & inhibitors*
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Phosphoprotein Phosphatases / chemistry
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Phosphoprotein Phosphatases / metabolism
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Protein Binding
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Sequence Homology, Amino Acid
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Structure-Activity Relationship
Substances
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Enzyme Inhibitors
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Okadaic Acid
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Phosphoprotein Phosphatases