The Primary Ligand-Binding Interaction At The Glp-1 Receptor Is Via The Putative Helix Of The Peptide Agonists

Title: The Primary Ligand-Binding Interaction At The Glp-1 Receptor Is Via The Putative Helix Of The Peptide Agonists

Volume: 11 Issue: 1

Author(s): Suleiman Al-Sabah and Dan Donnelly

Affiliation:

Keywords: Glp-1 Receptor, peptidereceptor, Trp-Cage motif, N-terminus

Abstract: The N-terminal domain of the GLP-1 receptor binds the putative helical region of the peptide agonists, GLP-1 and exendin-4. Here we demonstrate that this interaction also determines the magnitude of a separate interaction between the N-terminus of these peptides and the receptors core domain. Enhancing the pre-formation of the C-terminal Trp-Cage motif of exendin-4, a motif critical for high-affinity binding, results in no improvement in receptor affinity, suggesting that this motif forms after the initial peptidereceptor binding event.

Cite this article as:

Al-Sabah Suleiman and Donnelly Dan, The Primary Ligand-Binding Interaction At The Glp-1 Receptor Is Via The Putative Helix Of The Peptide Agonists, Protein & Peptide Letters 2004; 11 (1) . https://dx.doi.org/10.2174/0929866043478365