ArticleProtein science : a publication of the Protein Society2008
Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints.
Article in Protein science : a publication of the Protein Society, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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32 citing papers in PubMed, 99 citations in OpenAlex.
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- Probing Biomolecular Interactions with Paramagnetic Nuclear Magnetic Resonance Spectroscopy.Chembiochem : a European journal of chemical biology · 2025Review
- Neuroinflammation and galectins: a key relationship in neurodegenerative diseases.Glycoconjugate journal · 2022Review
- Lanthanide-Based Optical Probes of Biological Systems.Cell chemical biology · 2020Review
- Structural Aspects of Heparan Sulfate Binding to Robo1-Ig1-2.ACS chemical biology · 2016Article
- "Rules of Engagement" of Protein-Glycoconjugate Interactions: A Molecular View Achievable by using NMR Spectroscopy and Molecular Modeling.ChemistryOpen · 2016Review
- Identification of the Glycosaminoglycan Binding Site of Interleukin-10 by NMR Spectroscopy.The Journal of biological chemistry · 2016Article
- Paramagnetic NMR probes for characterization of the dynamic conformations and interactions of oligosaccharides.Glycoconjugate journal · 2015Review
- 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
- Paramagnetic relaxation enhancement of membrane proteins by incorporation of the metal-chelating unnatural amino acid 2-amino-3-(8-hydroxyquinolin-3-yl)propanoic acid (HQA).Journal of biomolecular NMR · 2015Article
- FANTEN: a new web-based interface for the analysis of magnetic anisotropy-induced NMR data.Journal of biomolecular NMR · 2015Article
- Simultaneous use of solution NMR and X-ray data in REFMAC5 for joint refinement/detection of structural differences.Acta crystallographica. Section D, Biological crystallography · 2014Article
- Protein structure validation and identification from unassigned residual dipolar coupling data using 2D-PDPA.Molecules (Basel, Switzerland) · 2013Article
- Protein-carbohydrate interactions studied by NMR: from molecular recognition to drug design.Current protein & peptide science · 2012Review
- Lanthanide binding and IgG affinity construct: potential applications in solution NMR, MRI, and luminescence microscopy.Protein science : a publication of the Protein Society · 2012Article
- Convenient method for resolving degeneracies due to symmetry of the magnetic susceptibility tensor and its application to pseudo contact shift-based protein-protein complex structure determination.Journal of biomolecular NMR · 2012Article
- Protein structure determination from pseudocontact shifts using ROSETTA.Journal of molecular biology · 2012Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
The determination of the location and conformation of a natural ligand bound to a protein receptor is often a first step in the rational design of molecules that can modulate receptor function. NMR observables, including NOEs, often provide the basis for these determinations. However, when ligands are carbohydrates, interactions mediated by extensive hydrogen-bonding networks often reduce or eliminate NOEs between ligand and protein protons. In these cases, it is useful to look to other distance- and orientation-dependent observables that can constrain the geometry of ligand-protein complexes. Here we illustrate the use of paramagnetism-based NMR constraints, including pseudo-contact shifts (PCS) and field-induced residual dipolar couplings (RDCs). When a paramagnetic center can be attached to the protein, field-induced RDCs and PCS reflect only bound-state properties of the ligand, even when averages over small fractions of bound states and large fractions of free states are observed. The effects can also be observed over a long range, making it possible to attach a paramagnetic center to a remote part of the protein. The system studied here is a Galectin-3-lactose complex. A lanthanide-binding peptide showing minimal flexibility with respect to the protein was integrated into the C terminus of an expression construct for the Galectin-3-carbohydrate-binding domain. Dysprosium ion, which has a large magnetic susceptibility anisotropy, was complexed to the peptide, making it possible to observe both PCSs and field-induced RDCs for the protein and the ligand. The structure determined from these constraints shows agreement with a crystal structure of a Galectin-3-N-acetyllactosamine complex.
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