Periodate-triggered cross-linking of DOPA-containing peptide-protein complexes
Periodate-triggered cross-linking of DOPA-containing peptide-protein complexes
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DOI：
10.1021/ja045982c
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发表时间：
2004-09-22
影响因子：
15
通讯作者：
Kodadek, T
中科院分区：
文献类型：
--
作者：
Burdine, L;Gillette, TG;Kodadek, T
化学交联是分析蛋白质-小分子和蛋白质-蛋白质相互作用的强大方法。我们描述了一种新的化学交联反应的蛋白质复合物的研究的发展。具体而言，我们表明，含有邻二羟基芳烃单元的分子可以被氧化选择性与高碘酸钠在天然蛋白质的存在下，产生邻醌中间体，可以与合适的附近的蛋白质残基交联。我们证明了这种化学方法对肽-蛋白复合物的有效性和特异性，并推导出蛋白酶体亚复合物上人工激活结构域的结合位点。
Chemical cross-linking is a powerful methodology for analyzing proteins−small molecule and protein−protein interactions. We describe the development of a new chemical cross-linking reaction for the study of protein complexes. Specifically, we show that molecules containing an ortho dihydroxyarene unit can be oxidized selectively with sodium periodate in the presence of native proteins, producing an ortho quinone intermediate that can cross-link with suitable nearby protein residues. We demonstrate the efficacy and specificity of this chemistry for a peptide−protein complex and also deduce the binding site of an artificial activation domain on a proteasome subcomplex.