Dopamine receptor divergence revealed using a common ligand.

Sibley, David R; Nilson, Ashley N; Moritz, Amy E; Shi, Lei

Sibley, David R; Nilson, Ashley N; Moritz, Amy E; Shi, Lei.

Afiliação

Sibley DR; Molecular Neuropharmacology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, 35 Convent Drive, Bethesda, MD 20892, USA. Electronic address: sibleyd@ninds.nih.gov.
Nilson AN; Molecular Neuropharmacology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, 35 Convent Drive, Bethesda, MD 20892, USA.
Moritz AE; Molecular Neuropharmacology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health, 35 Convent Drive, Bethesda, MD 20892, USA.
Shi L; Computational Chemistry and Molecular Biophysics Section, Molecular Targets and Medications Discovery Branch, National Institute on Drug Abuse, National Institutes of Health, 333 Cassell Drive, Baltimore, MD 21224, USA. Electronic address: lei.shi2@nih.gov.

Trends Pharmacol Sci ; 44(10): 637-639, 2023 10.

Article em En | MEDLINE | ID: mdl-37599183

ABSTRACT

ABSTRACT

Rational drug design for G protein-coupled receptors (GPCRs) remains a challenging area. A new study from the Xu, Roth, and Zhang groups provides a complete set of active structures for the entire dopamine receptor family bound with rotigotine that will aid in designing selective agonists for these important therapeutic targets.

Assuntos

Desenho de Fármacos; Receptores Dopaminérgicos; Humanos; Ligantes

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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Desenho de Fármacos / Receptores Dopaminérgicos Limite: Humans Idioma: En Ano de publicação: 2023 Tipo de documento: Article

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