Next Article in Journal
Biomarkers in Alzheimer’s Disease Analysis by Mass Spectrometry-Based Proteomics
Next Article in Special Issue
The G Protein-Coupled Receptor Heterodimer Network (GPCR-HetNet) and Its Hub Components
Previous Article in Journal
Treatment with Panax Ginseng Antagonizes the Estrogen Decline in Ovariectomized Mice
Previous Article in Special Issue
A Rapid and Efficient Immunoenzymatic Assay to Detect Receptor Protein Interactions: G Protein-Coupled Receptors
Article Menu

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2014, 15(5), 7841-7864; doi:10.3390/ijms15057841

Alpha-Bulges in G Protein-Coupled Receptors

Centre for Molecular and Biomolecular Informatics, Radboud University Medical Centre, Geert Grooteplein 26-28, 6525 GA Nijmegen, The Netherlands
Present address: Switch Laboratory, Department of Cellular and Molecular Medicine, University of Leuven, 3000 Leuven, Belgium
*
Author to whom correspondence should be addressed.
Received: 20 January 2014 / Revised: 2 April 2014 / Accepted: 9 April 2014 / Published: 6 May 2014
(This article belongs to the Collection G Protein-Coupled Receptor Signaling and Regulation)
View Full-Text   |   Download PDF [6168 KB, uploaded 19 June 2014]   |  

Abstract

Agonist binding is related to a series of motions in G protein-coupled receptors (GPCRs) that result in the separation of transmembrane helices III and VI at their cytosolic ends and subsequent G protein binding. A large number of smaller motions also seem to be associated with activation. Most helices in GPCRs are highly irregular and often contain kinks, with extensive literature already available about the role of prolines in kink formation and the precise function of these kinks. GPCR transmembrane helices also contain many α-bulges. In this article we aim to draw attention to the role of these α-bulges in ligand and G-protein binding, as well as their role in several aspects of the mobility associated with GPCR activation. This mobility includes regularization and translation of helix III in the extracellular direction, a rotation of the entire helix VI, an inward movement of the helices near the extracellular side, and a concerted motion of the cytosolic ends of the helices that makes their orientation appear more circular and that opens up space for the G protein to bind. In several cases, α-bulges either appear or disappear as part of the activation process. View Full-Text
Keywords: GPCR; π-helix; α-bulge; GPCR activation; random forest; structure-function GPCR; π-helix; α-bulge; GPCR activation; random forest; structure-function
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

van der Kant, R.; Vriend, G. Alpha-Bulges in G Protein-Coupled Receptors. Int. J. Mol. Sci. 2014, 15, 7841-7864.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top