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首页> 外文期刊>Biochemistry >THE PLECKSTRIN HOMOLOGY DOMAIN OF PHOSPHOLIPASE C-DELTA(1) BINDS WITH HIGH AFFINITY TO PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE IN BILAYER MEMBRANES
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THE PLECKSTRIN HOMOLOGY DOMAIN OF PHOSPHOLIPASE C-DELTA(1) BINDS WITH HIGH AFFINITY TO PHOSPHATIDYLINOSITOL 4,5-BISPHOSPHATE IN BILAYER MEMBRANES

机译：对双层膜中磷脂酰肌醇4,5-双磷酸酯具有高亲和力的磷脂酶C-DEL（1）结合的pleckstrin同源性域

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摘要

The pleckstrin homology (PH) domain of phospholipase C-delta(1) (PLC-delta(1)) binds to phosphatidylinositol 4,5-bisphosphate (PI(4,5)P-2) in phospholipid membranes with an affinity (K-a similar to 10(6) M(-1)) and specificity comparable to those of the native enzyme. PLC-delta(1) and its PH domain also bind inositol 1,4,5-trisphosphate, the polar head group of PI(4,5)P-2, with comparable affinity and approximately 1:1 stoichiometry. A peptide corresponding to amino acids 30-43 of the PLC-delta(1) PH domain contains several basic residues predicted to bind PI(4,5)P-2, but binds weakly and with little specificity for PI(4,5)P-2; hence the tertiary structure of the isolated PH domain is required for high affinity PI(4,5)P-2 binding. Our PI(4,5)P-2 binding results support the hypothesis that the intact PH domain, serving as' a specific tether, directs PLC-delta(1) to membranes enriched in PI(4,5)P-2 and permits the active site, located elsewhere in the protein, to hydrolyze multiple substrate molecules before this enzyme dissociates from the membrane surface.
机译：磷脂酶C-delta（1）（PLC-delta（1））的pleckstrin同源（PH）域以亲和力（Ka）与磷脂膜中的磷脂酰肌醇4,5-二磷酸（PI（4,5）P-2）结合与10（6）M（-1）相似，且特异性与天然酶相当。 PLC-delta（1）及其PH结构域还结合肌醇1,4,5-三磷酸（PI（4,5）P-2的极性头基），具有可比的亲和力和大约1：1的化学计量。与PLC-delta（1）PH域的氨基酸30-43相对应的肽含有几个预计会结合PI（4,5）P-2的基本残基，但结合较弱，对PI（4,5）的特异性很小P-2;因此，高亲和力PI（4,5）P-2结合需要分离的PH结构域的三级结构。我们的PI（4,5）P-2结合结果支持以下假设：完整的PH结构域充当特定的系链，将PLC-delta（1）引导至富含PI（4,5）P-2的膜并允许活性位点（位于蛋白质的其他位置）在该酶从膜表面解离之前水解多个底物分子。

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