Antibodies directed to restricted sequences of the c-Erb a α hinge domain interfere with hormone or dna binding to recombinant α-type triiodothyronine receptor (c-Erb a α1) and detect structural changes
| Autor: | Christelle Lenoir, Malika Daadi, Richard Planells, Enrico Macchia, Janine Torresani, Giorgilli G, J. Bonne |
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| Rok vydání: | 1995 |
| Předmět: |
Immunoprecipitation
Molecular Sequence Data Clinical Biochemistry Peptide Biology Biochemistry Antibodies law.invention Structure-Activity Relationship chemistry.chemical_compound law Complementary DNA Receptors Animals Thyroid Hormone Amino Acid Sequence Receptor Molecular Biology chemistry.chemical_classification Receptors Thyroid Hormone Binding Sites Base Sequence DNA Cell Biology Molecular biology Recombinant Proteins Rats Blot chemistry Recombinant DNA biology.protein Triiodothyronine Rabbits Antibody |
| Zdroj: | Journal of Receptors and Signal Transduction. 15:715-735 |
| ISSN: | 1532-4281 1079-9893 |
| DOI: | 10.3109/10799899509079902 |
| Popis: | In a previous study we showed that antibodies directed to restricted sequences in the hinge domain of α-type triiodothyronine (T3) receptor (TR) (aminoacids 150-166, 172-191, 144-162) selectively recognized and immunoprecipitated α-type TR in tissues. Furthermore, antibodies to peptide 172-191 (anti-α 172) strongly impaired T3 binding to natural TR α. To get more precise informations on the ability of these antibodies to recognize the TR, alter TR properties and/or detect conformational changes in TR, TR αl was produced in E. coli as a non-mutated, non-fusion protein from a rat c-erb A α1 cDNA inserted into pTrc99A vector. The recombinant c-Erb A αl protein, after solubilization with 5 M guanidine and progressive refolding, presented the main characteristics of TR α: unique or largely dominant band of 46 KDa in Western blots with the different anti-c-Erb A α antibodies; binding to DNA and to T3. Binding to DNA was markedly attenuated by anti-α 144 but not by anti-α 150 and anti-α 172. Binding to T... |
| Databáze: | OpenAIRE |
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