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A Protocol for Computer-Based Protein Structure and Function Prediction
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Apelinergic System Structure and Function.

Kyungsoo Shin1, Calem Kenward1, Jan K Rainey1,2

  • 1Department of Biochemistry & Molecular Biology, Dalhousie University, Halifax, Nova Scotia, Canada.

Comprehensive Physiology
|January 23, 2018
PubMed
Summary
This summary is machine-generated.

Apelin and apela peptides bind the apelin receptor (AR), influencing physiological processes. This review highlights how different peptide isoforms impact AR function, offering new therapeutic insights.

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Area of Science:

  • Physiology
  • Biochemistry
  • Pharmacology

Background:

  • Apelin and apela are peptide ligands for the apelin receptor (AR), a G-protein-coupled receptor.
  • Ligand-AR interactions are crucial for regulating the adipoinsular axis, cardiovascular, and central nervous systems.
  • Both apelin and apela exist in various endogenous isoforms, affecting receptor binding and activation.

Purpose of the Study:

  • To review the apelinergic system, focusing on structure-function correlations.
  • To emphasize the impact of ligand and receptor isoform-dependent properties.
  • To explore the potential for therapeutic regulation of the system.

Main Methods:

  • Literature review of the apelinergic system components.
  • Analysis of structure-function relationships for apelin and apela isoforms.
  • Discussion of biophysical and biological membrane-mediated receptor interactions.

Main Results:

  • Apelin and apela isoforms exhibit variable potency and efficacy.
  • Key structural motifs for apelin binding are identified.
  • The apelin receptor (AR) has been challenging to characterize biophysically, though recent structural data offers promise.

Conclusions:

  • The apelinergic system's regulation is complex, involving multiple ligands and isoforms.
  • Isoform-dependent pharmacological properties are critical for understanding system function.
  • Further biophysical studies are needed to fully elucidate AR mechanisms.