Topological analysis of the human beta 2-adrenergic receptor expressed in Escherichia coli.
AUTOR(ES)
Lacatena, R M
RESUMO
We have investigated the topology of the human beta 2-adrenergic receptor expressed in Escherichia coli, using the genetic method described by Beckwith and coworkers. We found that fusions with alkaline phosphatase beyond a certain point on the human beta 2-adrenergic receptor sequence were assembled into the bacterial membrane with the same topology as the human beta 2-adrenergic receptor in the mammalian membrane. The pattern that might have been expected on the basis of the topology of the human beta 2-adrenergic receptor in mammalian membranes was not reflected in the levels of alkaline phosphatase activity of the fusions occurring between the N-terminal region and positions close to the second external domain. Our data suggest that the correct positioning of the N terminus of the receptor depends on the presence of its C-terminal portions.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=45053Documentos Relacionados
- Mutational analysis of ligand binding activity of beta 2 adrenergic receptor expressed in Escherichia coli.
- Human beta 2-adrenergic receptors expressed in Escherichia coli membranes retain their pharmacological properties.
- Chromosomal assignment of the gene for the human beta 2-adrenergic receptor.
- Myocardial signaling defects and impaired cardiac function of a human beta 2-adrenergic receptor polymorphism expressed in transgenic mice.
- Structure of the gene for human beta 2-adrenergic receptor: expression and promoter characterization.
