Premium
Structural insights into the dynamic process of G‐protein– coupled receptor activation
Author(s) -
Kobilka Brian
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.323.1
Subject(s) - g protein coupled receptor , transmembrane domain , chemistry , receptor , transmembrane protein , biophysics , ligand (biochemistry) , g protein , microbiology and biotechnology , biology , biochemistry
GPCRs conduct the majority of transmembrane responses to hormones and neurotransmitters, and mediate the senses of sight, smell and taste. The β 2 AR adrenoceptor (β 2 AR) is a prototypical Family A GPCR that mediates physiologic responses to adrenaline and noradrenaline. We have obtained three‐dimensional structures of the β 2 AR in inactive and active conformations, as well as a structure of the β 2 AR in complex with the G protein Gs. We have also used fluorescence, EPR and NMR spectroscopy to study the dynamic properties of the receptor, and to map ligand‐specific conformational changes. I will discuss what we these studies have taught us about the structural basis of GPCR function.