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PUBMED FOR HANDHELDS

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  • Title: The primary ligand-binding interaction at the GLP-1 receptor is via the putative helix of the peptide agonists.
    Author: Al-Sabah S, Donnelly D.
    Journal: Protein Pept Lett; 2004 Feb; 11(1):9-14. PubMed ID: 14965273.
    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 receptor's 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 peptide-receptor binding event.
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