Isotope-coded and affinity-tagged cross-linking (ICATXL): An efficient strategy to probe protein interaction surfaces

被引:45
作者
Chu, Feixia [1 ]
Mahrus, Sami [1 ]
Craik, Charles S. [1 ]
Burlingame, Alma L. [1 ]
机构
[1] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA
关键词
D O I
10.1021/ja0614159
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Chemical cross-linking followed by identification of the cross-linked residues by mass spectrometry provides structural information on protein interaction surfaces. Nevertheless, accurate analysis of the digested, cross-linked proteins is often challenging. Herein, we describe a novel strategy that relies on the use of affinity-tagged cross-linkers and isotope coding on the cross-linker-modified species. Incorporation of O16 or O18 during the hydrolysis of the cross-linkers results in a characteristic "doublet" for the undesired products of a half-cross-linking reaction. Therefore, genuine cross-linked peptides are readily distinguished for further structural analysis. This strategy permits a sensitive and facile analysis on a dimeric protease inhibitor, ecotin, showing general applicability to other protein assemblies. Copyright © 2006 American Chemical Society.
引用
收藏
页码:10362 / 10363
页数:2
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