ArticleChembiochem : a European journal of chemical biology2019
Deriving Ligand Orientation in Weak Protein-Ligand Complexes by DEEP-STD NMR Spectroscopy in the Absence of Protein Chemical-Shift Assignment.
Article in Chembiochem : a European journal of chemical biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Native MS and ligand observed NMR uncovers subtle SLiM binding variations that mediate HSP90-Hop PPI modulation.RSC chemical biology · 2026Article
- NMR in the Age of Modern Biomedical Research and Drug Discovery.Journal of molecular biology · 2025Review
- Fast Quantitative Validation of 3D Models of Low-Affinity Protein-Ligand Complexes by STD NMR Spectroscopy.Journal of medicinal chemistry · 2024Article
- Glycosaminoglycans: What Remains To Be Deciphered?JACS Au · 2023Review
- Applications of Solution NMR in Drug Discovery.Molecules (Basel, Switzerland) · 2021Review
- Elucidation of a sialic acid metabolism pathway in mucus-foraging Ruminococcus gnavus unravels mechanisms of bacterial adaptation to the gut.Nature microbiology · 2019Article
- Structural Basis of Glycerophosphodiester Recognition by theACS chemical biology · 2019Article
- Deriving Ligand Orientation in Weak Protein-Ligand Complexes by DEEP-STD NMR Spectroscopy in the Absence of Protein Chemical-Shift Assignment.Chembiochem : a European journal of chemical biology · 2019Article
- Self-acetylation at the active site of phosphoenolpyruvate carboxykinase (PCK1) controls enzyme activity.The Journal of biological chemistryArticle
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5 authors.
Funding
Abstract
Differential epitope mapping saturation transfer difference (DEEP-STD) NMR spectroscopy is a recently developed powerful approach for elucidating the structure and pharmacophore of weak protein-ligand interactions, as it reports key information on the orientation of the ligand and the architecture of the binding pocket. The method relies on selective saturation of protein residues in the binding site and the generation of a differential epitope map by observing the ligand, which depicts the nature of the protein residues making contact with the ligand in the bound state. Selective saturation requires knowledge of the chemical-shift assignment of the protein residues, which can be obtained either experimentally by NMR spectroscopy or predicted from 3D structures. Herein, we propose a simple experimental procedure to expand the DEEP-STD NMR methodology to protein-ligand cases in which the spectral assignment of the protein is not available. This is achieved by experimentally identifying the chemical shifts of the residues present in binding hot-spots on the surface of the receptor protein by using 2D NMR experiments combined with a paramagnetic probe.
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