Engineering the Ligand Specificity of the Human Galectin-1 by Incorporation of Tryptophan Analogues
Language English Country Germany Media print-electronic
Document type Journal Article, Research Support, Non-U.S. Gov't
- Keywords
- lectins, molecular dynamics, non-canonical amino acids, protein engineering, synthetic glycobiology,
- MeSH
- Galectin 1 * chemistry MeSH
- Galectins metabolism MeSH
- Humans MeSH
- Ligands MeSH
- Oligosaccharides chemistry MeSH
- Tryptophan * MeSH
- Binding Sites MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Galectin 1 * MeSH
- Galectins MeSH
- Ligands MeSH
- Oligosaccharides MeSH
- Tryptophan * MeSH
Galectin-1 is a β-galactoside-binding lectin with manifold biological functions. A single tryptophan residue (W68) in its carbohydrate binding site plays a major role in ligand binding and is highly conserved among galectins. To fine tune galectin-1 specificity, we introduced several non-canonical tryptophan analogues at this position of human galectin-1 and analyzed the resulting variants using glycan microarrays. Two variants containing 7-azatryptophan and 7-fluorotryptophan showed a reduced affinity for 3'-sulfated oligosaccharides. Their interaction with different ligands was further analyzed by fluorescence polarization competition assay. Using molecular modeling we provide structural clues that the change in affinities comes from modulated interactions and solvation patterns. Thus, we show that the introduction of subtle atomic mutations in the ligand binding site of galectin-1 is an attractive approach for fine-tuning its interactions with different ligands.
cib Austrian Centre of Industrial Biotechnology Petersgasse 14 8010 Graz Austria
Department of Chemistry University of Karachi Karachi Pakistan
Institute of Molecular Biotechnology Graz University of Technology Petersgasse 14 8010 Graz Austria
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