| Autor: |
Obosi LA; School of Biological and Molecular Sciences, Oxford Brookes University, UK., Hen R, Beadle DJ, Bermudez I, King LA |
| Jazyk: |
angličtina |
| Zdroj: |
FEBS letters [FEBS Lett] 1997 Jul 28; Vol. 412 (2), pp. 321-4. |
| DOI: |
10.1016/s0014-5793(97)00813-2 |
| Abstrakt: |
The mouse serotonin (5-HT) receptor subtype, 5-HT7, belongs to the family of seven transmembrane G-protein-coupled receptors. To identify the structural basis for the coupling of 5-HT7 receptor to G alpha(s) we constructed a number of receptor mutants in which amino acid residues were either substituted or deleted from the second and third intracellular loops. Wild-type and mutant 5-HT7 receptors were expressed in insect cells using the baculovirus vectors. Two mutant receptor species, 5-HT7(E325G) and 5-HT7(K327S), demonstrated markedly impaired abilities to stimulate adenylyl cyclase. The results suggest the importance of the C-terminal region of the third intracellular loop in receptor-G-protein interaction and that specific charged residues, E325 and K327, may play a critical role in this interaction. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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