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Structural Basis of the Diversity of Adrenergic Receptors.

Abstract：

:Adrenergic receptors are highly homologous while at the same time display a wide diversity of ligand and G-protein binding, and understanding this diversity is key for designing selective or biased drugs for them. Here, we determine two crystal structures of the α2A adrenergic receptor (α2AAR) in complex with a partial agonist and an antagonist. Key non-conserved residues from the ligand-binding pocket (Phe7.39 and Tyr6.55) to G-protein coupling region (Ile34.51 and Lys34.56) are discovered to play a key role in the interplay between partial agonism and biased signaling of α2AAR, which provides insights into the diversity of ligand binding and G-protein coupling preference of adrenergic receptors and lays the foundation for the discovery of next-generation drugs targeting these receptors.

journal_name

Cell Rep

journal_title

Cell reports

authors

Qu L,Zhou Q,Xu Y,Guo Y,Chen X,Yao D,Han GW,Liu ZJ,Stevens RC,Zhong G,Wu D,Zhao S

doi

10.1016/j.celrep.2019.10.088

subject

Has Abstract

pub_date

2019-12-03 00:00:00

pages

2929-2935.e4

issue

10

issn

2211-1247

pii

S2211-1247(19)31410-X

journal_volume

29

pub_type

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