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Cell surface delivery and structural re-organization by pharmacological chaperones of an oligomerization-defective α(1b)-adrenoceptor mutant demonstrates membrane targeting of GPCR oligomers
Many G-protein-coupled receptors, including the α(1b)-adrenoceptor, form homo-dimers or oligomers. Mutation of hydrophobic residues in transmembrane domains I and IV alters the organization of the α(1b)-adrenoceptor oligomer, with transmembrane domain IV playing a critical role. These mutations also...
| Autores principales: | , , |
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| Formato: | Texto |
| Lenguaje: | English |
| Publicado: |
Portland Press Ltd.
2008
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| Materias: | |
| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2605960/ https://www.ncbi.nlm.nih.gov/pubmed/18764782 http://dx.doi.org/10.1042/BJ20081227 |