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Structure and Dynamics of the Human beta 2 Adrenoceptor
Author(s) -
Kobilka Brian K
Publication year - 2008
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.22.1_supplement.539.1
Subject(s) - g protein coupled receptor , receptor , chemistry , inverse agonist , biophysics , adrenergic receptor , function (biology) , beta adrenoceptor , microbiology and biotechnology , agonist , biochemistry , biology
G protein coupled receptors (GPCRs) are remarkably versatile signaling molecules. The beta 2 adrenoceptor (beta2AR) is a prototypical Family A GPCR that mediates physiologic responses to adrenaline and noradrenaline. The function of the beta2AR can be modulated by a spectrum of synthetic ligands ranging from full agonists to inverse agonists. We have used crystallography to determine the three‐dimensional structure of the beta2AR, and fluorescence spectroscopy to map ligand‐induced conformational changes and characterize the structure of beta2AR dimers. I will discuss what we these studies have taught us about the structural basis of beta2ARs function.