Effect of mutations in the beta1-thyroid hormone receptor on the inhibition of T3 binding by desethylamiodarone
| Autor: | H C van Beeren, Wilmar M. Wiersinga, V.K.K. Chatterjee, O. Bakker |
|---|---|
| Přispěvatelé: | Other departments |
| Jazyk: | angličtina |
| Rok vydání: | 1999 |
| Předmět: |
Molecular Sequence Data
Static Electricity Mutant Biophysics Amiodarone Mutant β1-thyroid hormone receptor Binding Competitive Biochemistry Structural Biology Genetics Humans Amino Acid Sequence Binding site Desethylamiodarone Molecular Biology chemistry.chemical_classification Receptors Thyroid Hormone Thyroid hormone receptor Triiodothyronine Sequence Homology Amino Acid Inhibition of triiodothyronine binding Wild type Cell Biology Amino acid chemistry Hormone receptor Mutation Helix Dimerization Protein Binding |
| Zdroj: | FEBS letters, 450(1-2), 35-38. Wiley-Blackwell |
| ISSN: | 0014-5793 |
| Popis: | Desethylamiodarone (DEA) acts as a competitive inhibitor of triiodothyronine (T3) binding to the alpha1-thyroid hormone receptor (TR alpha1) but as a non-competitive inhibitor with respect to TR beta1. To gain insight into the position of the binding site of desethylamiodarone on TR beta1 we investigated the naturally occurring mutants Y321C, R429Q, P453A, P453T and the artificial mutants L421R and E457A in the ligand binding domain of human TR beta1. The IC50 values (in microM) of DEA for P453A (50 +/- 11) and P453T (55 +/- 16) mutant TR beta1 are not different from that for the wild type TR beta1 (56 +/- 15), but the IC50 values of R429Q (32 +/- 7; P |
| Databáze: | OpenAIRE |
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