Protein-DNA and protein-hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor?
- PMID: 201845
- DOI: 10.1038/268115a0
Protein-DNA and protein-hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor?
Abstract
High resolution X-ray analysis of the hormone-binding protein prealbumin has shown that it has a structural complementarity to double-helical DNA. The proposed binding site is composed of two symmetry-related beta-sheets containing a pair of helically disposed arms, which can interact with the bases in the wide groove of DNA. A palindromic target sequence is indicated by the symmetry of the protein. The two identical thyroid hormone binding sites on prealbumin are located in a channel that runs completely through the molecule. These two structural features suggest prealbumin as a model for the thyroid hormone nuclear receptor, providing a number of detailed predictions of its properties.
Similar articles
-
Prealbumin and the thyroid hormone nuclear receptor.Proc R Soc Lond B Biol Sci. 1981 Mar 27;211(1185):413-31. doi: 10.1098/rspb.1981.0015. Proc R Soc Lond B Biol Sci. 1981. PMID: 6112755
-
Thyroid hormone interactions: molecular conformation, protein binding, and hormone action.Endocr Rev. 1980 Spring;1(2):140-66. doi: 10.1210/edrv-1-2-140. Endocr Rev. 1980. PMID: 6263601 Review. No abstract available.
-
Thyroid hormone binding to human serum prealbumin and rat liver nuclear receptor: kinetics, contribution of the hormone phenolic hydroxyl group, and accommodation of hormone side-chain bulk.Biochemistry. 1982 Jan 5;21(1):163-70. doi: 10.1021/bi00530a028. Biochemistry. 1982. PMID: 6277365 No abstract available.
-
Computer graphics in drug design: molecular modeling of thyroid hormone-prealbumin interactions.J Med Chem. 1982 Jul;25(7):785-90. doi: 10.1021/jm00349a004. J Med Chem. 1982. PMID: 7108895
-
Thyroxine transport proteins of plasma. Molecular properties and biosynthesis.Recent Prog Horm Res. 1978;34:477-519. doi: 10.1016/b978-0-12-571134-0.50017-x. Recent Prog Horm Res. 1978. PMID: 216060 Review. No abstract available.
Cited by
-
Regulation of activity of chromatin receptors for thyroid hormone: possible involvement of histone-like proteins.Proc Natl Acad Sci U S A. 1979 Oct;76(10):5005-9. doi: 10.1073/pnas.76.10.5005. Proc Natl Acad Sci U S A. 1979. PMID: 228271 Free PMC article.
-
A computer aided oligonucleotide analysis provides a model sequence for RNA polymerase-promoter recognition in E.coli.Nucleic Acids Res. 1978 Oct;5(10):3759-73. doi: 10.1093/nar/5.10.3759. Nucleic Acids Res. 1978. PMID: 364417 Free PMC article.
-
Electrostatic potential molecular surfaces.Proc Natl Acad Sci U S A. 1982 Jun;79(12):3754-8. doi: 10.1073/pnas.79.12.3754. Proc Natl Acad Sci U S A. 1982. PMID: 6285364 Free PMC article.
-
The supramolecular chemistry of β-sheets.J Am Chem Soc. 2013 Apr 17;135(15):5477-92. doi: 10.1021/ja3088407. Epub 2013 Apr 2. J Am Chem Soc. 2013. PMID: 23548073 Free PMC article. Review.
-
Sulfated metabolites of polychlorinated biphenyls are high-affinity ligands for the thyroid hormone transport protein transthyretin.Environ Health Perspect. 2013 Jun;121(6):657-62. doi: 10.1289/ehp.1206198. Epub 2013 Apr 12. Environ Health Perspect. 2013. PMID: 23584369 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials