Structural basis for Na+-sensitivity in dopamine D2 and D3 receptors

被引：27

作者：

Michino, Mayako ^{[1
,2
]}

Free, R. Benjamin ^{[3
]}

Doyle, Trevor B. ^{[3
]}

Sibley, David R. ^{[3
]}

Shi, Lei ^{[1
,2
,4
]}

机构：

[1] Cornell Univ, Weill Med Coll, Dept Physiol & Biophys, New York, NY 10021 USA

[2] NIDA, Computat Chem & Mol Biophys Unit, Intramural Res Program, NIH, Baltimore, MD USA

[3] NINDS, NIH, Mol Neuropharmacol Sect, Bethesda, MD 20892 USA

[4] Cornell Univ, Weill Med Coll, Inst Computat Biomed, New York, NY 10021 USA

来源：

CHEMICAL COMMUNICATIONS | 2015年 / 51卷 / 41期

关键词：

PROTEIN-COUPLED RECEPTORS; BINDING-SITE CREVICE; ALLOSTERIC MODULATION; SODIUM-BINDING; PIVOTAL ROLE; ANTAGONIST; INHIBITION; MEMBRANE; RESIDUES; AFFINITY;

D O I：

10.1039/c5cc02204e

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

To understand the structural basis for the Na+-sensitivity of ligand binding to dopamine D2-like receptors, using computational analysis in combination with binding assays, we identified interactions critical in propagating the impact of Na+ on receptor conformations and on the ligand-binding site. Our findings expand the pharmacologically-relevant conformational spectrum of these receptors.

引用

页码：8618 / 8621

页数：4

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