3-DIMENSIONAL STRUCTURE OF THE CATALYTIC SUBUNIT OF PROTEIN SERINE/THREONINE PHOSPHATASE-1
3-DIMENSIONAL STRUCTURE OF THE CATALYTIC SUBUNIT OF PROTEIN SERINE/THREONINE PHOSPHATASE-1
复制标题
DOI：
10.1038/376745a0
复制
发表时间：
1995-08-31
期刊：
影响因子：
64.8
通讯作者：
KURIYAN, J
中科院分区：
文献类型：
--
作者：
GOLDBERG, J;HUANG, HB;KURIYAN, J
哺乳动物蛋白磷酸酶-1的晶体结构，与毒素微囊藻毒素和确定在2.1埃分辨率，揭示了它是一种金属酶无关的建筑酪氨酸磷酸酶。两个金属离子通过中心β-α-β-α-β支架定位在活性位点，从活性位点发出三个表面凹槽，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以调节功能。预期催化结构域的折叠在蛋白磷酸酶2A和2B（钙调磷酸酶）中被紧密地保留。
The crystal structure of mammalian protein phosphatase-1, complexed with the toxin microcystin and determined at 2.1 Angstrom 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).