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Vu, Oanh [Author]; Bender, Brian Joseph [Author]; Pankewitz, Lisa [Author]; Huster, Daniel [Author]; Beck-Sickinger, Annette G. [Author]; Meiler, Jens [Author]

The Structural Basis of Peptide Binding at Class A G Protein-Coupled Receptors

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  • Media type: E-Article
  • Title: The Structural Basis of Peptide Binding at Class A G Protein-Coupled Receptors
  • Contributor: Vu, Oanh [Author]; Bender, Brian Joseph [Author]; Pankewitz, Lisa [Author]; Huster, Daniel [Author]; Beck-Sickinger, Annette G. [Author]; Meiler, Jens [Author]
  • Published: Basel: MDPI, [2023]
  • Published in: Molecules ; 27,1, (2022)
  • Language: English
  • Keywords: peptide docking ; class A GPCR ; peptide GPCR ; non-canonical amino acids
  • Origination:
  • Footnote:
  • Description: G protein-coupled receptors (GPCRs) represent the largest membrane protein family and a significant target class for therapeutics. Receptors from GPCRs’ largest class, class A, influence virtually every aspect of human physiology. About 45% of the members of this family endogenously bind flexible peptides or peptides segments within larger protein ligands. While many of these peptides have been structurally characterized in their solution state, the few studies of peptides in their receptor-bound state suggest that these peptides interact with a shared set of residues and undergo significant conformational changes. For the purpose of understanding binding dynamics and the development of peptidomimetic drug compounds, further studies should investigate the peptide ligands that are complexed to their cognate receptor.
  • Access State: Open Access
  • Rights information: Attribution (CC BY)