Lanthanide-tagged proteins - an illuminating partnership

被引：97

作者：

Allen, Karen N. ^{[1
]}

Imperiali, Barbara ^{[2
,3
]}

机构：

[1] Boston Univ, Dept Chem, Boston, MA 02215 USA

[2] MIT, Dept Chem, Cambridge, MA 02139 USA

[3] MIT, Dept Biol, Cambridge, MA 02139 USA

来源：

CURRENT OPINION IN CHEMICAL BIOLOGY | 2010年 / 14卷 / 02期

关键词：

BINDING TAGS; ENERGY-TRANSFER; PARAMAGNETIC NMR; HIGH-AFFINITY; LUMINESCENCE; PEPTIDE; TERBIUM; DELIVERY; DESIGN; SITE;

D O I：

10.1016/j.cbpa.2010.01.004

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Lanthanide-tagged proteins are valuable for exploiting the unique properties of Ln ions for investigating protein structure, function, and dynamics. Introduction of the Ln into the target is accomplished via chemical modification with synthetic lanthanide-chelating prosthetic groups or by coexpression with peptide-based binding tags. Complexed Ln-tags offer a heavy-atom site for solving the phase problem in X-ray crystallography In NMR, paramagnetic lanthanide ions induce residual dipolar couplings and pseudo-contact shifts that yield valuable distance constraints for structural analysis. Lanthanide luminescence-based techniques and Ln-tagged proteins are valuable for investigating the functions and dynamics of large proteins and protein complexes and have been applied in vivo. Overall, the reach of Ln-tagged proteins will increase our ability to understand cellular functions on the molecular level.

引用

页码：247 / 254

页数：8

共 38 条

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