Molecular Neurobiology

, Volume 19, Issue 2, pp 111–149

Structural features of heterotrimeric G-protein-coupled receptors and their modulatory proteins

  • Harry LeVine

DOI: 10.1007/BF02743657

Cite this article as:
LeVine, H. Mol Neurobiol (1999) 19: 111. doi:10.1007/BF02743657


Over the past 20 years, the general mechanism for signaling through 7-transmembrane helix receptors coupled to GTP hydrolysis has been worked out. Although similar in overall organization, subtype variability and subcellular localization of components have built in considerable signaling specificity. Atomic resolution structures for many of the components have delineated the domain organization of these complex proteins and have given physical form to the idea of subtype specificity. This review describes what is known about the physical structures of the 7-transmembrane helix receptors, the heterotrimeric GTP binding coupling proteins, the adenylate cyclase and phospholipase C effector proteins, and signaling modulatory proteins, such as arrestin, phosducin, recoverin-type myristoyl switch proteins, and the pleckstrin homology domain of G-protein receptor kinase-2. These images allow experimenters to contemplate the details of the supramolecular organization of the multiprotein complexes involved in the transmission of signals across the cellular lipid bilayer.

Index Entries

X-ray structuresNMR, reconstitutionpeptidesarrestinphosducinG-protein receptor kinasesRGS proteinsadenylate cyclasephospholipase C

Copyright information

© Humana Press Inc. 1999

Authors and Affiliations

  • Harry LeVine
    • 1
  1. 1.Parke-Davis Pharmaceutical Research Division of Warner-Lambert CompanyAnn Arbor