Structural basis of G protein-coupled receptor function

Mol Cell Endocrinol. 1999 May 25;151(1-2):181-93. doi: 10.1016/s0303-7207(99)00017-9.


The vast majority of extracellular signaling molecules, like hormones and neurotransmitters, interact with a class of membranous receptors characterized by a uniform molecular architecture of seven transmembrane alpha-helices linked by extra- and intracelluar peptide loops. In a reversible manner, binding of diverse agonists to heptahelical receptors leads to activation of a limited repertoire of heterotrimeric guanine nucleotide-binding proteins (G proteins) forwarding the signal to intracellular effectors such as enzymes and ion channels. Proper functioning of a G protein-coupled receptor is based on a complex interplay of structural determinants which are ultimately responsible for receptor folding, trafficking and transmembrane signaling. Applying novel biochemical and molecular biological methods interesting insights into receptor structure/function relationships became available. These studies have a significant impact on our understanding of the molecular basis of human diseases and may eventually lead to novel therapeutic strategies.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • GTP-Binding Proteins / metabolism*
  • Humans
  • Protein Conformation
  • Receptors, Cell Surface / chemistry*
  • Receptors, Cell Surface / metabolism*
  • Signal Transduction
  • Structure-Activity Relationship


  • Receptors, Cell Surface
  • GTP-Binding Proteins