Three recent articles published in Cell1,2 and Cell Research3 have reported multiple cryo-electron microscopy(cryo-EM)structures of the D1 dopamine receptor(DRD1)bound to either dopamine,various DRD1 agonists,or a pos...Three recent articles published in Cell1,2 and Cell Research3 have reported multiple cryo-electron microscopy(cryo-EM)structures of the D1 dopamine receptor(DRD1)bound to either dopamine,various DRD1 agonists,or a positive allosteric modulator(PAM),while in complex with the active heterotrimeric Gs protein.These studies describe for the first time active-state structures of the DRD1,an exciting advancement in the field that will allow for a better understanding of selective agonist binding,DRD1 activation,G protein selectivity,and the provision of multiple templates to facilitate future drug design and discovery for this important therapeutic target.展开更多
基金the Intramural Research Programs of the National Institute of Neurological Disorders(ZIA-NS002263)Stroke and the National Institute on Drug Abuse(Z1A DA000609).
文摘Three recent articles published in Cell1,2 and Cell Research3 have reported multiple cryo-electron microscopy(cryo-EM)structures of the D1 dopamine receptor(DRD1)bound to either dopamine,various DRD1 agonists,or a positive allosteric modulator(PAM),while in complex with the active heterotrimeric Gs protein.These studies describe for the first time active-state structures of the DRD1,an exciting advancement in the field that will allow for a better understanding of selective agonist binding,DRD1 activation,G protein selectivity,and the provision of multiple templates to facilitate future drug design and discovery for this important therapeutic target.
