Protein-DNA and protein-hormone interactions in prealbumin: a model of the thyroid hormone nuclear receptor?
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.
D000595:Amino Acid Sequence; D001665:Binding Sites; D002467:Cell Nucleus / Q000378:metabolism; D003461:Crystallography; D004247:DNA / Q000378:metabolism*; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011228:Prealbumin / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism*; D013963:Thyroid Hormones / Q000378:metabolism*; D013974:Thyroxine / Q000378:metabolism
D011228:Prealbumin; D011956:Receptors, Cell Surface; D012709:Serum Albumin; D013963:Thyroid Hormones; D004247:DNA; D013974:Thyroxine