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在细胞膜上挣扎:磷脂信号传导的结构视角

Floundering about at cell membranes: a structural view of phospholipid signaling.

作者信息

Hurley J H, Tsujishita Y, Pearson M A

机构信息

Laboratory of Molecular Biology, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD 20892-0580, USA.

出版信息

Curr Opin Struct Biol. 2000 Dec;10(6):737-43. doi: 10.1016/s0959-440x(00)00144-5.

DOI:10.1016/s0959-440x(00)00144-5
PMID:11114512
Abstract

Structures are now available for the majority of the enzyme families involved in the phosphorylation, dephosphorylation and hydrolysis of signaling phospholipids. Lipid kinase and phosphatase structures recapitulate catalytic motifs involved in protein phosphorylation and dephosphorylation, whereas cytosolic phospholipase A(2) manifests novel catalytic geometry. Structures have been determined for most known intracellular phospholipid 'receptor' domains, both those that bind membrane-embedded phospholipids and those that bind lipid monomers.

摘要

目前,参与信号磷脂磷酸化、去磷酸化和水解的大多数酶家族的结构已为人所知。脂质激酶和磷酸酶的结构概括了参与蛋白质磷酸化和去磷酸化的催化基序,而胞质磷脂酶A(2)则呈现出新颖的催化几何结构。对于大多数已知的细胞内磷脂“受体”结构域,包括那些结合膜嵌入磷脂的结构域和那些结合脂质单体的结构域,其结构均已确定。

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