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• W1488257827 startingPage "789" @default.
• W1488257827 abstract "Glucagon binding to and recognition by its cell surface receptor is the necessary first step in the cascade of events leading to the activation of adenylate cyclase by the hormone. It has long been presumed that glucagon adopts an ordered conformation upon binding to its membrane-bound receptor. A recent model of this three-dimensional structure based on biophysical data, predicts beta-turns at positions 2-5, 10-13, and 15-18, and an alpha-helical region between residues 19-27. Our approach in the design of antagonists of glucagon was to elucidate the steric and electronic features that stabilize these secondary structures to obtain analogs that bind with high affinity to the receptor but do not activate adenylate cyclase. Nineteen glucagon analogs incorporating structural changes at the amino-terminal sequence 1-5, at positions 9 and 12, and at the carboxyl-terminal helical region were synthesized. Des-His1-[Glu9]glucagon amide was recently shown to be a competitive inhibitor. Our synthetic studies in combination with this modification have resulted in seven new glucagon antagonists. The implications for the structural and conformational properties required for binding and activity of glucagon and the glucagon peptide family are discussed." @default.
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• W1488257827 date "1989-01-01" @default.
• W1488257827 modified "2023-09-30" @default.
• W1488257827 title "Glucagon Antagonists: Contribution to Binding and Activity of the Amino-terminal Sequence 1–5, Position 12, and the Putative α-Helical Segment 19–27" @default.
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• W1488257827 doi "https://doi.org/10.1016/s0021-9258(19)85011-1" @default.
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• W1488257827 hasPublicationYear "1989" @default.
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