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Binding Domain Characterization of Growth Hormone Secretagogue Receptor.

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|August 12, 2022
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Synthetic agonists MK-0677 and GHS-25 show higher growth hormone (GH) release than ghrelin. The growth hormone secretagogue receptor (GHS-R) binding pocket involves transmembrane domain 6 and specific amino acids, crucial for ligand interaction.

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Area of Science:

  • Endocrinology
  • Molecular Biology
  • Pharmacology

Background:

  • The ghrelin receptor (GHS-R) regulates growth hormone (GH) release and appetite.
  • GHS-R is a G-protein coupled receptor with significant therapeutic potential.
  • Understanding GHS-R ligand interactions is key for developing new GHS-R targeted therapies.

Purpose of the Study:

  • To characterize the binding and functional properties of GHS-R with synthetic agonists and ghrelin.
  • To identify the structural determinants of the GHS-R ligand-binding pocket.

Main Methods:

  • Radiolabeled ligand-binding and GH release assays.
  • Aequorin-based intracellular calcium ([Ca2+]i) measurements.
  • GHS-R chimera analysis and site-directed mutagenesis.

Main Results:

  • Synthetic agonists MK-0677 and GHS-25 exhibited high binding affinity and superior in vivo GH secretagogue activity compared to ghrelin.
  • GHS-R knockout mice showed abolished activity, confirming specificity.
  • Transmembrane domain 6 (TM6) and specific residues (D99, W276) were identified as critical for ligand binding and activity.
  • Distinct residues (E124 for MK-0677, F279 for ghrelin/GHS-25) mediate differential ligand interactions.

Conclusions:

  • The GHS-R ligand-binding pocket is primarily defined by residues in TM6 and surrounding regions.
  • This detailed structural and functional understanding facilitates the design of novel GHS-R modulators for therapeutic applications.