Cargando…
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 D(2) and D(3) receptors (D(2)R and D(3)R), we find that eticlopride binds D(2)R in a pose very similar to that in the D(3)R/eticlopride structure but incompatible with the D(2)R/risperidone structure. In addition, r...
Autores principales: | Lane, J Robert, Abramyan, Ara M, Adhikari, Pramisha, Keen, Alastair C, Lee, Kuo-Hao, Sanchez, Julie, Verma, Ravi Kumar, Lim, Herman D, Yano, Hideaki, Javitch, Jonathan A, Shi, Lei |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2020
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7053997/ https://www.ncbi.nlm.nih.gov/pubmed/31985399 http://dx.doi.org/10.7554/eLife.52189 |
Ejemplares similares
-
Chirality of Novel Bitopic Agonists Determines Unique Pharmacology at the Dopamine D3 Receptor
por: Adhikari, Pramisha, et al.
Publicado: (2021) -
FLEXIQuant-LF to quantify protein modification extent in label-free proteomics data
por: Schlaffner, Christoph N, et al.
Publicado: (2020) -
Regulating G protein-coupled receptors by topological inversion
por: Denard, Bray, et al.
Publicado: (2019) -
The E(2.65)A mutation disrupts dynamic binding poses of SB269652 at the dopamine D2 and D3 receptors
por: Verma, Ravi Kumar, et al.
Publicado: (2018) -
Ligand recognition and biased agonism of the D1 dopamine receptor
por: Teng, Xiao, et al.
Publicado: (2022)