Serine/threonine phosphatases: mechanism through structure.
摘要：
The reversible phosphorylation of proteins is accomplished by opposing activities of kinases and phosphatases. Relatively few protein serine/threonine phosphatases (PSPs) control the specific dephosphorylation of thousands of phosphoprotein substrates. Many PSPs, exemplified by protein phosphatase 1 (PP1) and PP2A, achieve substrate specificity and regulation through combinatorial interactions between conserved catalytic subunits and a large number of regulatory subunits. Other PSPs, represented by PP2C and FCP/SCP, contain both catalytic and regulatory domains within the same polypeptide chain. Here, we discuss biochemical and structural investigations that advance the mechanistic understanding of the three major classes of PSPs, with a focus on PP2A.
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关键词：
Animals Humans Phosphoprotein Phosphatases Protein Phosphatase 1 Protein Phosphatase 2 Models, Molecular
DOI：
10.1016/j.cell.2009.10.006
被引量：
年份：
2009
Elsevier
Elsevier
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掌桥科研
Semantic Scholar
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万方医学
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