共 35 条
An engineered aryl azide ligase for site-specific mapping of protein-protein interactions through photo-cross-linking
被引:71
作者:

Baruah, Hemanta
论文数: 0 引用数: 0
h-index: 0
机构:
MIT, Dept Chem, Cambridge, MA 02139 USA MIT, Dept Chem, Cambridge, MA 02139 USA

Puthenveetil, SuJiet
论文数: 0 引用数: 0
h-index: 0
机构:
MIT, Dept Chem, Cambridge, MA 02139 USA MIT, Dept Chem, Cambridge, MA 02139 USA

Choi, Yoon-Aa
论文数: 0 引用数: 0
h-index: 0
机构:
MIT, Dept Chem, Cambridge, MA 02139 USA MIT, Dept Chem, Cambridge, MA 02139 USA

Shah, Samit
论文数: 0 引用数: 0
h-index: 0
机构:
MIT, Dept Chem, Cambridge, MA 02139 USA MIT, Dept Chem, Cambridge, MA 02139 USA

Ting, Alice Y.
论文数: 0 引用数: 0
h-index: 0
机构:
MIT, Dept Chem, Cambridge, MA 02139 USA MIT, Dept Chem, Cambridge, MA 02139 USA
机构:
[1] MIT, Dept Chem, Cambridge, MA 02139 USA
关键词:
ligases;
photo-cross-linking;
protein engineering;
protein interactions;
site-specific labeling;
D O I:
10.1002/anie.200802088
中图分类号:
O6 [化学];
学科分类号:
0703 ;
摘要:
(Chemical Equation Presented) Labeled and linked: The small-molecule binding site of Escherichia coli lipoic acid ligase was re-engineered to accept a fluorinated aryl azide probe in place of lipoic acid. Labeling with this mutant is highly specific for LAP fusion proteins. In cell lysate, FK506 binding protein was labeled and rapamycin-dependent photocross-linking to its interaction partner was demonstrated. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.
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页码:7018 / 7021
页数:4
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