Structure of the dopamine D<sub>2</sub> receptor in complex with the antipsychotic drug spiperone.

Im, Dohyun; Inoue, Asuka; Fujiwara, Takaaki; Nakane, Takanori; Yamanaka, Yasuaki; Uemura, Tomoko; Mori, Chihiro; Shiimura, Yuki et al. · Nat Commun · 2020

basic_science · Level V

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Abstract

In addition to the serotonin 5-HT<sub>2A</sub> receptor (5-HT<sub>2A</sub>R), the dopamine D<sub>2</sub> receptor (D<sub>2</sub>R) is a key therapeutic target of antipsychotics for the treatment of schizophrenia. The inactive state structures of D<sub>2</sub>R have been described in complex with the inverse agonists risperidone (D<sub>2</sub>R<sub>ris</sub>) and haloperidol (D<sub>2</sub>R<sub>hal</sub>). Here we describe the structure of human D<sub>2</sub>R in complex with spiperone (D<sub>2</sub>R<sub>spi</sub>). In D<sub>2</sub>R<sub>spi</sub>, the conformation of the extracellular loop (ECL) 2, which composes the ligand-binding pocket, was substantially different from those in D<sub>2</sub>R<sub>ris</sub> and D<sub>2</sub>R<sub>hal</sub>, demonstrating that ECL2 in D<sub>2</sub>R is highly dynamic. Moreover, D<sub>2</sub>R<sub>spi</sub> exhibited an extended binding pocket to accommodate spiperone's phenyl ring, which probably contributes to the selectivity of spiperone to D<sub>2</sub>R and 5-HT<sub>2A</sub>R. Together with D<sub>2</sub>R<sub>ris</sub> and D<sub>2</sub>R<sub>hal</sub>, the structural information of D<sub>2</sub>R<sub>spi</sub> should be of value for designing novel antipsychotics with improved safety and efficacy.

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