Goldberg J, Huang H B, Kwon Y G, Greengard P, Nairn A C, Kuriyan J
Howard Hughes Medical Institute, Rockefeller University, New York, New York 10021, USA.
Nature. 1995 Aug 31;376(6543):745-53. doi: 10.1038/376745a0.
The crystal structure of mammalian protein phosphatase-1, complexed with the toxin microcystin and determined at 2.1 A resolution, reveals that it is a metalloenzyme unrelated in architecture to the tyrosine phosphatases. Two metal ions are positioned by a central beta-alpha-beta-alpha-beta scaffold at the active site, from which emanate three surface grooves that are potential binding sites for substrates and inhibitors. The carboxy terminus is positioned at the end of one of the grooves such that regulatory sequences following the domain might modulate function. The fold of the catalytic domain is expected to be closely preserved in protein phosphatases 2A and 2B (calcineurin).
与毒素微囊藻毒素复合并以2.1埃分辨率测定的哺乳动物蛋白磷酸酶-1的晶体结构表明，它是一种金属酶，其结构与酪氨酸磷酸酶无关。两个金属离子由位于活性位点的中央β-α-β-α-β支架定位，从该支架发出三个表面凹槽，这些凹槽是底物和抑制剂的潜在结合位点。羧基末端位于其中一个凹槽的末端，使得该结构域之后的调节序列可能调节功能。催化结构域的折叠预计在蛋白磷酸酶2A和2B（钙调神经磷酸酶）中得到紧密保留。
