ArticleChemistry & biology2007
Spin-labeled analogs of CMP-NeuAc as NMR probes of the alpha-2,6-sialyltransferase ST6Gal I.
Article in Chemistry & biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Review
- Investigation of Strand-Selective Interaction of SNA-Modified siRNA with AGO2-MID.International journal of molecular sciences · 2020Article
- NMR Resonance Assignment Methodology: Characterizing Large Sparsely Labeled Glycoproteins.Journal of molecular biology · 2019Article
- Direct determination of multiple ligand interactions with the extracellular domain of the calcium-sensing receptor.The Journal of biological chemistry · 2014Article
- Sparse labeling of proteins: structural characterization from long range constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Review
- Nuclear magnetic resonance structural characterization of substrates bound to the alpha-2,6-sialyltransferase, ST6Gal-I.Biochemistry · 2009Article
- NMR resonance assignments of sparsely labeled proteins: amide proton exchange correlations in native and denatured states.Journal of the American Chemical Society · 2009Article
- 13C-sialic acid labeling of glycans on glycoproteins using ST6Gal-I.Journal of the American Chemical Society · 2008Article
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7 authors at 1 institution in 1 country.
Funding
Abstract
Structural data on mammalian proteins are often difficult to obtain by conventional NMR approaches because of an inability to produce samples with uniform isotope labeling in bacterial expression hosts. Proteins with sparse isotope labels can be produced in eukaryotic hosts by using isotope-labeled forms of specific amino acids, but structural analysis then requires information from experiments other than nuclear Overhauser effects. One source of alternate structural information is distance-dependent perturbation of spin relaxation times by nitroxide spin-labeled analogs of natural protein ligands. Here, we introduce spin-labeled analogs of sugar nucleotide donors for sialyltransferases, specifically, CMP-TEMPO (CMP-4-O-[2,2,6,6-tetramethylpiperidine-1-oxyl]) and CMP-4carboxyTEMPO (CMP-4-O-[4-carboxy-2,2,6,6-tetramethylpiperidinine-1-oxyl]). An ability to identify resonances from active site residues and produce distance constraints is illustrated on a (15)N phenylalanine-labeled version of the structurally uncharacterized, alpha-2,6-linked sialyltransferase, ST6Gal I.
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