Distinct inactive conformations of the dopamine D2 and D3 receptors correspond to different extents of inverse agonism

Distinct inactive conformations of the dopamine D2 and D3 receptors correspond to different extents of inverse agonism

By analyzing and simulating inactive conformations of the highly homologous dopamine D2 and D3 receptors (D2R and D3R), we find that eticlopride binds D2R in a pose very similar to that in the D3R/eticlopride structure but incompatible with the D2R/risperidone structure. In addition, risperidone occ...

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Bibliographic Details
Main Authors: J Robert Lane, Ara M Abramyan, Pramisha Adhikari, Alastair C Keen, Kuo-Hao Lee, Julie Sanchez, Ravi Kumar Verma, Herman D Lim, Hideaki Yano, Jonathan A Javitch, Lei Shi
Format: Article
Language:English
Published: eLife Sciences Publications Ltd 2020-01-01
Series:eLife
Subjects:
dopamine d2 receptor
na+ sensitivity
inverse agonism
molecular dynamics
Online Access:https://elifesciences.org/articles/52189

Internet

https://elifesciences.org/articles/52189

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