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Public Library of Science, PLoS ONE, 8(7), p. e42023, 2012

DOI: 10.1371/journal.pone.0042023

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Membrane-Sensitive Conformational States of Helix 8 in the Metabotropic Glu2 Receptor, a Class C GPCR

Journal article published in 2012 by Agostino Bruno, Gabriele Costantino, Gianni de Fabritiis ORCID, G. De Fabritis, Manuel Pastor, Jana Selent ORCID, J. Salent
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

The recent elucidation of the x-ray structure of several class A GPCRs has clearly indicated that the amphipathic helix 8 (H8) is a conserved structural domain in most crystallized GPCRs. Very little is known about the presence and the possible role of an analogous H8 domain in the distantly related class C GPCRs. In this study, we investigated the structural properties for the H8 domain of the mGluR2 receptor, a class C GPCR, by applying extended molecular dynamics simulations. Our study indicates that the amphipathic H8 adopts membrane-sensitive conformational states which depend on the membrane composition. Cholesterol-rich membranes stabilize the helical structure of H8 whereas cholesterol-depleted membranes induce a disruption of H8. The observed link between membrane cholesterol levels and H8 conformational states suggests that H8 behaves as a sensor of cholesterol concentration