ArticleJournal of biomolecular NMR2011
An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe.
Article in Journal of biomolecular NMR, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Paramagnetic relaxation enhancement NMR as a tool to probe guest binding and exchange in metallohosts.Nature communications · 2022Article
- Conformational ensemble of a multidomain protein explored by GdBiophysical journal · 2021Article
- Phosphoserine for the generation of lanthanide-binding sites on proteins for paramagnetic nuclear magnetic resonance spectroscopy.Magnetic resonance (Gottingen, Germany) · 2021Article
- Paramagnetic NMR in drug discovery.Journal of biomolecular NMR · 2020Review
- Integrative Protein Modeling in RosettaNMR from Sparse Paramagnetic Restraints.Structure (London, England : 1993) · 2019Article
- Localization of ligands within human carbonic anhydrase II usingChemical science · 2019Article
- Methyl group reorientation under ligand binding probed by pseudocontact shifts.Journal of biomolecular NMR · 2018Article
- Investigating Protein-Ligand Interactions by Solution Nuclear Magnetic Resonance Spectroscopy.Chemphyschem : a European journal of chemical physics and physical chemistry · 2018Review
- Fast NMR Screening of Macromolecular Complexes by a Paramagnetic Spin Relaxation Filter.ACS omega · 2018Article
- Current NMR Techniques for Structure-Based Drug Discovery.Molecules (Basel, Switzerland) · 2018Review
- A new carbamidemethyl-linked lanthanoid chelating tag for PCS NMR spectroscopy of proteins in living HeLa cells.Journal of biomolecular NMR · 2016Article
- Process of Fragment-Based Lead Discovery-A Perspective from NMR.Molecules (Basel, Switzerland) · 2016Review
- Identification of the Glycosaminoglycan Binding Site of Interleukin-10 by NMR Spectroscopy.The Journal of biological chemistry · 2016Article
- Ligand-driven conformational changes of MurD visualized by paramagnetic NMR.Scientific reports · 2015Article
- Paramagnetic Ligand Tagging To Identify Protein Binding Sites.Journal of the American Chemical Society · 2015Article
- Information content of long-range NMR data for the characterization of conformational heterogeneity.Journal of biomolecular NMR · 2015Article
- Integral membrane protein structure determination using pseudocontact shifts.Journal of biomolecular NMR · 2015Article
- Compact, hydrophilic, lanthanide-binding tags for paramagnetic NMR spectroscopy.Chemical science · 2015Article
- FANTEN: a new web-based interface for the analysis of magnetic anisotropy-induced NMR data.Journal of biomolecular NMR · 2015Article
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6 authors.
Funding
Abstract
A nuclear magnetic resonance-based ligand screening strategy utilizing a paramagnetic lanthanide probe is presented. By fixing a paramagnetic lanthanide ion to a target protein, a pseudo-contact shift (PCS) and a paramagnetic relaxation enhancement (PRE) can be observed for both the target protein and its bound ligand. Based on PRE and PCS information, the bound ligand is then screened from the compound library and the structure of the ligand-protein complex is determined. PRE is an isotropic paramagnetic effect observed within 30 Å from the lanthanide ion, and is utilized for the ligand screening in the present study. PCS is an anisotropic paramagnetic effect providing long-range (~40 Å) distance and angular information on the observed nuclei relative to the paramagnetic lanthanide ion, and utilized for the structure determination of the ligand-protein complex. Since a two-point anchored lanthanide-binding peptide tag is utilized for fixing the lanthanide ion to the target protein, this screening method can be generally applied to non-metal-binding proteins. The usefulness of this strategy was demonstrated in the case of the growth factor receptor-bound protein 2 (Grb2) Src homology 2 (SH2) domain and its low- and high-affinity ligands.
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