Protein serine/threonine phosphatases

In the past year, the three-dimensional structures of two serine/threonine phosphatases, protein phosphatase-1 and protein phosphatase-2b (calcineurin), have been determined. The new information puts previous sequence comparisons and mutagenesis studies into a detailed structural perspective. The ac...

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Veröffentlicht in:	Current opinion in biotechnology 1996-08, Vol.7 (4), p.397-402
Hauptverfasser:	Ernest Villafranca, J, Kissinger, Charles R, Parge, Hans E
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Calcineurin Calmodulin-Binding Proteins - chemistry Calmodulin-Binding Proteins - genetics Crystallography, X-Ray Models, Molecular Molecular Sequence Data Phosphoprotein Phosphatases - chemistry Phosphoprotein Phosphatases - classification Phosphoprotein Phosphatases - genetics Phosphoprotein Phosphatases - physiology Protein Conformation Protein Engineering Protein Phosphatase 1 Recombinant Proteins - chemistry Recombinant Proteins - genetics Serine - metabolism Threonine - metabolism
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Beschreibung
Zusammenfassung:	In the past year, the three-dimensional structures of two serine/threonine phosphatases, protein phosphatase-1 and protein phosphatase-2b (calcineurin), have been determined. The new information puts previous sequence comparisons and mutagenesis studies into a detailed structural perspective. The active-site structure and catalytic mechanism appear to be common to a variety of phosphoesterase enzymes.
ISSN:	0958-1669 1879-0429
DOI:	10.1016/S0958-1669(96)80114-5