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外文期刊>The biochemical journal
>Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1
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Identification of the separate domains in the hepatic glycogen-targeting subunit of protein phosphatase 1 that interact with phosphorylase a, glycogen and protein phosphatase 1
pDeletion and mutational analyses of the rat liver glycogen-targeting subunit (GsubL/sub) of protein phosphatase 1 (PP1) have identified three separate domains that are responsible for binding of PP1, glycogen and phosphorylase ia/i. The glycogen-binding domain spans the centre of GsubL/sub between residues 144 and 231 and appears to be distinct from the glycogen-binding (storage) site of phosphorylase. The regulatory high-affinity binding site for phosphorylase ia/i lies in the 16 amino acids at the C-terminus of GsubL/sub. The PP1-binding domain is deduced to comprise the -RVXF- motif [Egloff, Johnson, Moorhead, Cohen and Barford (1997) EMBO J. b16/b, 1876–1887] located at residues 61–64 of GsubL/sub and preceding lysine residues at positions 56, 57 and 59. A possible approach for increasing glycogen synthesis in certain disorders is discussed./p
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机译：>蛋白磷酸酶1（PP1）的大鼠肝糖原靶向亚基（G L ）的缺失和突变分析确定了三个独立的域，这些域负责PP1，糖原和磷酸化酶的结合< i> a 。糖原结合结构域跨越残基144和231之间的G L 的中心，并且似乎与磷酸化酶的糖原结合（存储）位点不同。磷酸化酶 a 的调节性高亲和力结合位点位于G L 的C端的16个氨基酸。推测PP1结合域包含-RVXF-基序[Egloff，Johnson，Moorhead，Cohen and Barford（1997）EMBO J. 16 ，1876-1887]，位于-残基的61-64位。 G L 及其之前的赖氨酸残基位于56、57和59位。探讨了在某些疾病中增加糖原合成的可能方法。
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