This is an accepted version of a paper published in Molecular membrane biology. This paper has been peer-reviewed but does not include the final publisher proof-corrections or journal pagination.Citation for the published paper: Jurkowski, W., Yazdi, S., Elofsson, A. (2013)
AbstractThe 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 di erent binding properties to other molecules and e ects on intracellular signaling. To gain insight on the molecular basis of receptor subtype speci ficity, we have generated a three-dimensional model for each of the galanin receptors based on its homologs in the same family. We found significant di erences in the organization of the binding pockets among the three types of receptors, which might be the key for specific molecular recognition o igands. Through docking o ragments of the galanin peptide and a number o igands, we investigated the involvement of transmembrane and loop residues in ligand interaction.