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Structural basis for signal recognition and transduction by platelet-activating-factor receptor.

Abstract：

:Platelet-activating-factor receptor (PAFR) responds to platelet-activating factor (PAF), a phospholipid mediator of cell-to-cell communication that exhibits diverse physiological effects. PAFR is considered an important drug target for treating asthma, inflammation and cardiovascular diseases. Here we report crystal structures of human PAFR in complex with the antagonist SR 27417 and the inverse agonist ABT-491 at 2.8-Å and 2.9-Å resolution, respectively. The structures, supported by molecular docking of PAF, provide insights into the signal-recognition mechanisms of PAFR. The PAFR-SR 27417 structure reveals an unusual conformation showing that the intracellular tips of helices II and IV shift outward by 13 Å and 4 Å, respectively, and helix VIII adopts an inward conformation. The PAFR structures, combined with single-molecule FRET and cell-based functional assays, suggest that the conformational change in the helical bundle is ligand dependent and plays a critical role in PAFR activation, thus greatly extending knowledge about signaling by G-protein-coupled receptors.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Cao C,Tan Q,Xu C,He L,Yang L,Zhou Y,Zhou Y,Qiao A,Lu M,Yi C,Han GW,Wang X,Li X,Yang H,Rao Z,Jiang H,Zhao Y,Liu J,Stevens RC,Zhao Q,Zhang XC,Wu B

doi

10.1038/s41594-018-0068-y

subject

Has Abstract

pub_date

2018-06-01 00:00:00

pages

488-495

issue

6

eissn

1545-9993

issn

1545-9985

pii

10.1038/s41594-018-0068-y

journal_volume

25

pub_type

杂志文章

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