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MINIREVIEW: Interactions Among a Subfamily of Nuclear Hormone Receptors: The Regulatory Zipper Model
Author(s) -
Barry M. Forman,
Herbert H. Samuels
Publication year - 1990
Publication title -
molecular endocrinology
Language(s) - English
Resource type - Journals
eISSN - 1944-9917
pISSN - 0888-8809
DOI - 10.1210/mend-4-9-1293
Subject(s) - biology , nuclear receptor , transcription factor , zinc finger , subfamily , receptor , leucine zipper , zipper , bzip domain , microbiology and biotechnology , pelp 1 , small heterodimer partner , dna binding protein , gene , genetics , computer science , algorithm
The nuclear hormone receptors comprise a superfamily of ligand-modulated transcription factors that regulate homeostasis, reproduction, development, and differentiation. Three amino acids within the zinc finger DNA binding motif determine target gene specificity. Groups of receptors exist with similar DNA binding specificity. A complex carboxy terminal region mediates ligand binding, dimerization, and hormone-relieved transcriptional inactivation. We summarize the current understanding of these phenomena and suggest a novel model that structurally and functionally links these events. This "regulatory zipper model" may explain the mechanism by which ligand activates nuclear hormone receptors.

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