By Gerald Litwack (Eds.)
Steroids is a thematic quantity from the vintage educational Press sequence, Vitamins and Hormones . Gerald Litwack, the hot editor of this prestigious serial, brings jointly major participants to the examine of steroids. those structurally and functionally complicated molecules are of curiosity to a vast cross-section of endocrinologist, telephone biologists, and biochemists. experiences comprise reports of constitution, functionality, and legislation of steroid construction and motion. hence, Vitamins and Hormones maintains to submit state of the art reports of curiosity to endocrinologists and biochemists. Others will more and more flip to this carrying on with sequence for accomplished studies by means of major researchers during this and comparable disciplines.
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Extra info for Advances in Research and Applications: Steroids
Many mutations have now been identified from DNA sequencing, and a data base is now developing (Fig. 15). The effects of the mutations in the DNA-binding domain can be understood with reference to the crystal structures of the GRdbd/GRE and ERdbd/ERE complexes. Given the structural similarity of the DBDs of receptors for glucocorticoid, retinoic acid p, estrogen, and 9-cis-retinoic acid, this modeling is likely to be sufficiently accurate to explain the mutational effects. Many of the substitutions in the vitamin D and androgen receptor DBDs involve residues that are conserved throughout the superfamily and, based on the GRdbd/GRE and ERdbd/ERE structures, are contacting bases or the phosphate backbone of the nucleic acid.
The sequence conservation of the Ti ligand-binding domain is apparent, but homology is much weaker for the dimerization subdomain. Nonetheless, it is clear that the dimerization region is rich in leucine and other small hydrophobic residues. 14. (A) Schematic illustrating the subdomains of the ligand-binding region. The amino end of the domain is to the left. (B) Sequence alignment of the Ti and dimerization regions of the ligand-binding domain. The figure is patterned in part on the alignment of Laudet et al.
Sigler, personal communication). The retinoic acid receptor preferentially activates reporter genes under the control of an element composed of ERE half-sites arranged as direct repeats with a spacing of five bases. , 1991). , 1993). , in a head-to-tail fashion). This is illustrated with a model of two DBDs bound to a direct repeat (Figs. 12 and 13). The model suggests that a hVDR homodimer or hVDR/RXR heterodimer could form protein-protein contacts through the DNA-binding domain when bound to a direct repeat with a threebase spacer (DR+3).
Advances in Research and Applications: Steroids by Gerald Litwack (Eds.)