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Updated: May 16, 2026

Disentangling Glycan-Protein Interactions: Nuclear Magnetic Resonance (NMR) to the Rescue
Published on: May 17, 2024
Ligand binding properties of human galanin receptors
Wiktor Jurkowski1, Samira Yazdi, Arne Elofsson
1Center for Biomembrane Research, Stockholm Bioinformatics Center, Department of Biochemistry and Biophysics, Science for Life Laboratory, Stockholm University, Stockholm, Sweden.
Abstract:
The galanin receptor family comprises of three members, GalR1, GalR2 and GalR3, all belonging to the G-protein-couple receptor superfamily. All three receptors bind the peptide hormone galanin, but show distinctly different binding properties to other molecules and effects on intracellular signaling. To gain insight on the molecular basis of receptor subtype specificity, we have generated a three-dimensional model for each of the galanin receptors based on its homologs in the same family. We found significant differences in the organization of the binding pockets among the three types of receptors, which might be the key for specific molecular recognition of ligands. Through docking of fragments of the galanin peptide and a number of ligands, we investigated the involvement of transmembrane and loop residues in ligand interaction.
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