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KMID : 0578320150380020105
Molecules and Cells
2015 Volume.38 No. 2 p.105 ~ p.111
Structural Features of ¥â2 Adrenergic Receptor: Crystal Structures and Beyond
Bang In-Jin

Choi Hee-Jung
Abstract
The beta2-adrenergic receptor (¥â2AR) family, which is the largest family of cell surface receptors in humans. Extra attention has been focused on the human GPCRs because they have been studied as important protein targets for pharmaceutical drug development. In fact, approximately 40% of marketed drugs directly work on GPCRs. GPCRs respond to various extracellular stimuli, such as sensory signals, neurotransmitters, chemokines, and hormones, to induce structural changes at the cytoplasmic surface, activating downstream signaling pathways, primarily through interactions with heterotrimeric G proteins or through G-protein independent pathways, such as arrestin. Most GPCRs, except for rhodhopsin, which contains covalently linked 11 cis-retinal, bind to diffusible ligands, having various conformational states between inactive and active structures. The first human GPCR structure was determined using an inverse agonist bound ¥â2AR in 2007 and since then, more than 20 distinct GPCR structures have been solved. However, most GPCR structures were solved as inactive forms, and an agonist bound fully active structure is still hard to obtain. In a structural point of view, ¥â2AR is relatively well studied since its fully active structure as a complex with G protein as well as several inactive structures are available. The structural comparison of inactive and active states gives an important clue in understanding the activation mechanism of ¥â2AR. In this review, structural features of inactive and active states of ¥â2AR, the interaction of ¥â2AR with heterotrimeric G protein, and the comparison with ¥â1AR will be discussed.
KEYWORD
beta2-adrenergic receptor (¥â2AR), conformational change, crystal structure, G-protein coupled receptor (GPCR), heterotrimeric G protein
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