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首页> 外文期刊>Molecular and Cellular Biology >Genetic analysis of a phosphatidylinositol 3-kinase SH2 domain reveals determinants of specificity.
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Genetic analysis of a phosphatidylinositol 3-kinase SH2 domain reveals determinants of specificity.

机译：磷脂酰肌醇3-激酶SH2域的遗传分析揭示了特异性的决定因素。

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摘要

Phosphatidylinositol 3-kinase is an important element in both normal and oncogenic signal transduction. Polyomavirus middle T antigen transforms cells in a manner depending on association of its tyrosine 315 phosphorylation site with Src homology 2 (SH2) domains on the p85 subunit of the phosphatidylinositol 3-kinase. Both nonselective and site-directed mutagenesis have been used to probe the interaction of middle T with the N-terminal SH2 domain of p85. Most of the 24 mutants obtained showed reduced middle T binding. However, mutations that showed increased binding were also found. Comparison of middle T binding to that of the platelet-derived growth factor receptor showed that some mutations altered the specificity of recognition by the SH2 domain. Mutations altering S-393, D-394, and P-395 were shown to affect the ability of the SH2 domain to select peptides from a degenerate phosphopeptide library. These results focus attention on the role of the EF loop in the SH2 domain in determining binding selectivity at the third position after the phosphotyrosine.
机译：磷脂酰肌醇3-激酶是正常和致癌信号转导中的重要元素。多瘤病毒中间T抗原以其酪氨酸315磷酸化位点与磷脂酰肌醇3-激酶p85亚基上的Src同源2（SH2）域关联的方式转化细胞。非选择性诱变和定点诱变都已被用来探测中间T与p85 N末端SH2结构域的相互作用。获得的24个突变体中的大多数显示出降低的中间T结合。然而，还发现了显示结合增加的突变。比较中间T与血小板衍生的生长因子受体的结合，发现某些突变改变了SH2结构域识别的特异性。已显示改变S-393，D-394和P-395的突变会影响SH2域从简并的磷酸肽文库中选择肽的能力。这些结果集中在SH2域中的EF环在确定磷酸酪氨酸后第三个位置的结合选择性中的作用上。

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