Abstract
Recent structural information suggests that the HC(X)5R active-site motif defines three distinct evolutionary families of phosphatases that employ a common catalytic mechanism. In two instances, regulation of phosphatase activity employs autoinhibitory mechanisms involving either intermolecular or intramolecular interactions, whereby inhibition is mediated by sterically blocking the active-site cleft.
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.
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Review
MeSH terms
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Binding Sites / physiology*
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Biological Evolution*
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Catalytic Domain / physiology*
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Cell Cycle Proteins / chemistry
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Cell Cycle Proteins / metabolism
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Crystallography, X-Ray
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Dual Specificity Phosphatase 1
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Immediate-Early Proteins / chemistry
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Immediate-Early Proteins / metabolism
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Intracellular Signaling Peptides and Proteins
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Phosphoprotein Phosphatases*
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Protein Phosphatase 1
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases / chemistry
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Protein Tyrosine Phosphatases / metabolism*
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Receptor-Like Protein Tyrosine Phosphatases, Class 4
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Receptors, Cell Surface / chemistry
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Receptors, Cell Surface / metabolism
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SH2 Domain-Containing Protein Tyrosine Phosphatases
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Thiosulfate Sulfurtransferase / chemistry
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Thiosulfate Sulfurtransferase / metabolism
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src Homology Domains / physiology
Substances
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Cell Cycle Proteins
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Immediate-Early Proteins
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Intracellular Signaling Peptides and Proteins
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Receptors, Cell Surface
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Thiosulfate Sulfurtransferase
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Phosphoprotein Phosphatases
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Protein Phosphatase 1
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Dual Specificity Phosphatase 1
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases
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Receptor-Like Protein Tyrosine Phosphatases, Class 4
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SH2 Domain-Containing Protein Tyrosine Phosphatases