Journal
FEBS LETTERS
Volume 553, Issue 3, Pages 342-346Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(03)01043-3
Keywords
G protein-coupled receptor; receptor; agonist; glucagon-like peptide-1; antagonist; exendin
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Lysine-288 in the glucagon-like peptide-1 receptor was predicted to be ideally positioned to play a role in hormone binding. Subsequent mutation of Lys-288 to Ala or Leu greatly reduced hormone affinity, while substitution with Arg had minimal effect. Compared to wild type, the Lys288-Ala receptor had a reduced affinity for three peptide ligands with complete N-terminal sequences but not for their N-truncated analogues. Hence, the role of this positively charged residue, which is conserved at the equivalent position in all other Family B receptors, was determined to be important for receptor interaction with the N-terminal eight residues of peptide agonists. (C) 2003 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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