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Form and function in protein dephosphorylation

Article Abstract:

Protein dephosphorylation is a chemical reaction involved in the regulation of physiological processes such as glycogen metabolism, signal transduction, and osmoregulation. There are two classes of enzymes that regulate protein dephosphorylation: protein kinases and protein phosphatases. The latter are further subdivided into two, metallo-protein phosphatases and protein tyrosine phosphatases. An overview of the structure and function of these enzymes is presented.

Author: Denu, John M., Dixon, Jack E., Stuckey, Jeanne A., Saper, Mark A.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
Phosphorylation

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Structure of protein phosphatase 2A core enzyme bound to tumor-inducing toxins

Article Abstract:

The crystal structures of the protein phosphatase 2A (PP2A) core enzyme bound to two of its inhibitors, the tumor-inducing agents okadaic acid and microcystin-LR, at 2.6 and 2.8 Angstrom resolution respectively are reported. The scaffolding subunit exhibits considerable conformational flexibility, which is proposed to play an important role in PP2A function.

Author: Yigong Shi, Jeffrey, Philip D., Yongna Xing, Yanhui Xu, Yu Chen, Chao, Yang, Lin, Zheng, Li, Zhu, Strack, Stefan, Stock, Jeffrey B.
Publisher: Elsevier B.V.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 2006
Science & research, Proteins, Crystals, Crystal structure, Protein structure, Structure

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Subjects list: Research, Phosphatases
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