By Gerald Litwack (Eds.)

Steroids is a thematic quantity from the vintage educational Press sequence, Vitamins and Hormones . Gerald Litwack, the recent editor of this prestigious serial, brings jointly best participants to the learn 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 law of steroid creation and motion. hence, Vitamins and Hormones maintains to post state-of-the-art experiences of curiosity to endocrinologists and biochemists. Others will more and more flip to this carrying on with sequence for complete stories via major researchers during this and comparable disciplines.

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It is itself butressed by the con- STEROIDlNUCLEAR RECEPTORS 39 served Ser9. In the ERdbd this is in turn hydrogen-bonded to Glu19 (which contacts a cytosine base, see foregoing discussion). In the GMbd the serine is hydrogen-bonded to the peptide backbone. This network is clearly important for reinforcing the phosphate anchor such that any substitution of the conserved His12 would perturb the complex. VI. CONCLUSIONS The crystal structures of the GR and ER DBD/DNA complexes have provided stereochemical details of protein-DNA and protein-protein interactions, and the importance of these contacts have been corroborated by mutational analyses.

Using the P-box to group steroidhuclear receptors, two principal subgroups emerge, the members of which presumably recognize the same response element half-site. , the glucocorticoid, progesterone, mineralocorticoid, and androgen receptors). , estrogen, thyroid hormone, retinoic acid, ecdysone, and vitamin D, receptors) all appear to bind the ERE half-site (5’-AGGTCA-3’). Probably in all of these latter cases, the interaction is similar to that found in the ERdbd/ERE half-site, with the Glu of the P-Box accepting a hydrogen bond from the C of the complementary strand, tgaCct and making watermediated contacts to the A of tgAct, and Lys26 contacting both the G and T of agGTca.

87, 1123-1126. Marks, M. , Segars, J. , Driggers, P. , and Ozato, K. (1992). H-2RIIBP expressed from a baculovirus vector binds to multiple hormone response elements. Mol. Endocrinol. 6, 219-230. , and Harrison, S. C. (1992). DNA recognition by GAL4: Structure of a prokidDNA complex. Nature (London) 356,408-414. , and Gronemeyer, H. (1990). Agonistic and antagonistic activities of RU486 on the functions of the human progesterone receptor. EMBO J. 9, 3923-3932.

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Advances in Research and Applications: Steroids by Gerald Litwack (Eds.)
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