| Autor: |
Christoph Gruber, Simon Keuerleber, Michael Freissmuth, Ingrid Gsandtner, Jürgen Zezula, Patrick Thurner |
| Rok vydání: |
2012 |
| Předmět: |
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| Zdroj: |
BMC Pharmacology & Toxicology |
| ISSN: |
2050-6511 |
| DOI: |
10.1186/2050-6511-13-s1-a81 |
| Popis: |
Background The A2A adenosine receptor is of interest because of several reasons. (i) It is a frequently blocked pharmacological target, because it is the site of action of caffeine. (ii) It has a long C-terminus that provides a docking site for several proteins, which direct the fate of the receptor from its synthesis to its lysosomal degradation. (iii) The A2A receptor can only promote activation of a limited number of available Gs molecules. This coupling mode was termed restricted collision coupling. (iv) Most G protein-coupled receptors carry one or several cysteine residues in their C-terminus which is subject to palmitoylation to anchor and stabilize the amphipathic helix 8; the A2A receptor lacks this palmitoylation site. We explored the hypothesis that there is a causal link between the absence of a palmitoyl moiety and restricted collision coupling. |
| Databáze: |
OpenAIRE |
| Externí odkaz: |
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