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• W2163223185 endingPage "811" @default.
• W2163223185 startingPage "804" @default.
• W2163223185 abstract "Galanin is a neuropeptide found throughout the central and peripheral nervous systems of a wide range of species, ranging from human and mouse to frog and tuna. Galanin mediates its physiological roles through three receptors (GalR1–3), all members of the G-protein coupled receptor family. In mapping these roles, receptor subtype selective ligands are crucial tools. To facilitate the ligand design, data on receptor structure and interaction points are of great importance. The current study investigates the mechanism by which galanin interacts with GalR3. Mutated receptors were tested with competitive binding analysis in vitro. Our studies identify six mutagenic constructs that lost receptor affinity completely, despite being expressed at the cell surface. Mutations of the Tyr1033.33 in transmembrane helix (TM) III, His2516.51 in TM VI, Arg2737.35 or His2777.39 in TM VII, Phe2636.63 or Tyr2707.32 in the extracellular loop III all result in complete reduction of ligand binding. In addition, docking studies of an in silico model of GalR3 propose that four of the identified residues interact with pharmacophores situated within the galanin(2–6) sequence. This study provides novel insights into the interaction between ligands and GalR3 and highlights the requirement for correct design of targeting ligands." @default.
• W2163223185 created "2016-06-24" @default.
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• W2163223185 date "2010-12-01" @default.
• W2163223185 modified "2023-10-17" @default.
• W2163223185 title "Determining receptor–ligand interaction of human galanin receptor type 3" @default.
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• W2163223185 doi "https://doi.org/10.1016/j.neuint.2010.08.018" @default.
• W2163223185 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/20817064" @default.
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