Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates

YuK.R.; KimY.J.; JungS.-K.KuB.ParkH.ChoS.Y.JungH.ChungS.J.BaeK.H.LeeS.C.KimB.Y.EriksonR.L.RyuS.E.KimS.J.

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Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates

机译：脱去磷酸结构基础对phosphatidylinositide PTPRQ活动基板

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Unlike other classical protein tyrosine phosphatases (PTPs), PTPRQ (PTP receptor type Q) has dephosphorylating activity towards phosphatidylinositide (PI) substrates. Here, the structure of the catalytic domain of PTPRQ was solved at 1.56 ? resolution. Overall, PTPRQ adopts a tertiary fold typical of other classical PTPs. However, the disordered M6 loop of PTPRQ surrounding the catalytic core and the concomitant absence of interactions of this loop with residues in the PTP loop results in a flat active-site pocket. On the basis of structural and biochemical analyses, it is proposed that this structural feature might facilitate the accommodation of large substrates, making it suitable for the dephosphorylation of PI substrates. Moreover, subsequent kinetic experiments showed that PTPRQ has a strong preferences for PI(3,4,5)P3 over other PI substrates, suggesting that its regulation of cell survival and proliferation reflects downregulation of Akt signalling.

机译：与其他古典蛋白质酪氨酸磷酸酶(中)、PTPRQ (PTP受体类型问)已经脱去磷酸活动phosphatidylinositide(π)基质。PTPRQ的催化域的结构在1.56解决了吗?采用三级褶皱典型的其他经典中,。周围的催化核心和伴随缺乏互动的循环残留在PTP循环的结果在一个平面活性位点的口袋里。和生化分析、建议这个结构特征可能促进住宿的大型基板,使它适合的去磷酸化π基板。实验表明,PTPRQ有很强的偏好π(3、4、5)比其他πP3基板,这表明监管细胞生存和扩散的反映downregulation Akt的信号。

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《Acta crystallographica.Section D. Biological crystallography》 |2013年第8期|1522-1529|共8页
作者
YuK.R.; KimY.J.; JungS.-K.KuB.ParkH.ChoS.Y.JungH.ChungS.J.BaeK.H.LeeS.C.KimB.Y.EriksonR.L.RyuS.E.KimS.J.;
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作者单位

Department of Bioscience and Biotechnology, Sejong University, 98 Kunja-dong, Kwangjin-ku, Seoul;

College of Pharmacy, Chung-Ang University, Seoul 156-756, South Korea;

Department of Chemistry, College of Natural Science, Dongguk University, 26, Pil-dong 3-ga, Jung-guDepartment of Bio Engineering, Hanyang University, Seongdong-gu, Seoul 133-791, South KoreaChemical Biology Research Center, Korea Research Institute of Bioscience and Biotechnology, 111Department of Applied Biochemistry, Konkuk University, Danwol-dong 322, Chungju, Chungbuk 380-701Medical Proteomics Research Center, Korea Research Institute of Bioscience and Biotechnology, 111;

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中图分类化学;
关键词
Structural properties; Catalytic Domain; cell viabilityProtein Tyrosine PhosphatasesAKT Signaling PathwayCell SurvivalPhosphatidylinositolsDephosphorylation;

机译：结构特性;催化域;细胞viabilityProtein酪氨酸PhosphatasesAKT信号PathwayCellSurvivalPhosphatidylinositolsDephosphorylation;

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Structural basis for the dephosphorylating activity of PTPRQ towards phosphatidylinositide substrates

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