Structural Insights into the Process of GPCR-G Protein Complex Formation.
Cell
; 177(5): 1243-1251.e12, 2019 05 16.
Article
em En
| MEDLINE
| ID: mdl-31080070
ABSTRACT
The crystal structure of the ß2-adrenergic receptor (ß2AR) bound to the G protein adenylyl cyclase stimulatory G protein (Gs) captured the complex in a nucleotide-free state (ß2AR-Gsempty). Unfortunately, the ß2AR-Gsempty complex does not provide a clear explanation for G protein coupling specificity. Evidence from several sources suggests the existence of a transient complex between the ß2AR and GDP-bound Gs protein (ß2AR-GsGDP) that may represent an intermediate on the way to the formation of ß2AR-Gsempty and may contribute to coupling specificity. Here we present a structure of the ß2AR in complex with the carboxyl terminal 14 amino acids from Gαs along with the structure of the GDP-bound Gs heterotrimer. These structures provide evidence for an alternate interaction between the ß2AR and Gs that may represent an intermediate that contributes to Gs coupling specificity.
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Texto completo:
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Modelos Moleculares
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Adenilil Ciclases
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Receptores Adrenérgicos beta 2
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Subunidades alfa Gs de Proteínas de Ligação ao GTP
Limite:
Humans
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article