NMR Applications for Identifying β-TrCP Protein-Ligand Interactions

被引：4

作者：

Pons, J. ^{[1
]}

Tanchou, V. ^{[2
]}

Girault, J. -P. ^{[1
]}

Bertho, G. ^{[1
]}

Evrard-Todeschi, N. ^{[1
]}

机构：

[1] Univ Paris 05, Lab Chim & Biochim Pharmacol & Toxicol, CNRS, UMR 8601, F-75270 Paris 06, France

[2] CEA ValRho, Direct Sci Vivant, Inst Biol Environm & Biotechnol, Serv Biochim & Toxicol Nucl, F-30207 Bagnols Sur Ceze, France

来源：

MINI-REVIEWS IN MEDICINAL CHEMISTRY | 2011年 / 11卷 / 04期

关键词：

STD-NMR; WaterLOGSY; epitope mapping; docking; phosphorylated peptide; beta-TrCP complex; binding fragment; KAPPA-B-ALPHA; TRANSFER-DIFFERENCE NMR; HIGH-AFFINITY LIGANDS; COMPETITION STD-NMR; BINDING-AFFINITY; MAGNETIZATION-TRANSFER; DEPENDENT DEGRADATION; DESTRUCTION MOTIF; PHOSPHORYLATION; UBIQUITINATION;

D O I：

10.2174/138955711795305344

中图分类号：

R914 [药物化学];

学科分类号：

100701 ;

摘要：

In the absence of crystallographic data, NMR has emerged as the best way to define protein-ligand interactions. Using NMR experiments based on magnetization transfer, one can sort bound from unbound molecules, estimate the dissociation constant, identify contacts implied in the binding, characterize the structure of the bound ligand and conduct ligand competition assays.

引用

页码：283 / 297

页数：15

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