Conversion of the human 5-HT1Dβ serotonin receptor to the rat 5-HT1b ligand-binding phenotype by Thr355 ASN site directed mutagenesis
| Autor: | Mark W. Hamblin, Robert W. McGuffin, Mark A. Metcalf |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Threonine
Molecular Sequence Data Biology Biochemistry Cell Line Animals Humans 5-HT5A receptor Amino Acid Sequence Asparagine Binding site Receptor Site-directed mutagenesis 5-HT receptor Pharmacology chemistry.chemical_classification Binding Sites Molecular biology Recombinant Proteins Rats Amino acid Phenotype chemistry Pindolol Receptors Serotonin Mutagenesis Site-Directed |
| Zdroj: | Biochemical Pharmacology. 44:1917-1920 |
| ISSN: | 0006-2952 |
| DOI: | 10.1016/0006-2952(92)90092-w |
| Popis: | The human 5-HT 1Ds serotonin receptor and its rat homolog (also called the 5-HT 1B receptor) share 93% amino acid identity, yet display markedly different pharmacological specificities. Comparison of deduced amino acid sequences among these and other recently cloned receptors suggested that this phenotypic difference might be attributable to a single human threonine 355 /rat asparagine 351 amino acid difference in the putative seventh membrane spanning regions. We now report that Thr 355 Asn mutagenesis of the human S-HT 1Ds receptor alters the binding characteristics of the recombinant receptor in [ 3 H]5-HT binding assays to a profile very similar to that of the rat S-HT 1B binding site. These results confirm that this single amino acid difference is responsible for the majority of the known pharmacological discrepancies between human and rat observed for 5-HT 1Ds (S-HT 1B ) receptors. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|