Abstract
Nuclear receptors are organized into distinct functional domains, of which the most conserved is a 66-amino-acid DNA-binding domain (DBD) (1). This region, in some cases together with its C-terminal extension into the hinge region, imparts the receptor's ability to bind to target DNA sequences and form the appropriate cooperative homodimeric or heterodimeric complexes (2-6). Important advances in understanding DNA recognition has come from the direct visualization of the protein-DNA complexes, which can be achieved through X-ray diffraction studies ((7-12), as well as through other structural and biophysical methods that directly probe the DNA-binding surface of nuclear receptors (13-(17).
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Chasse, S.A., Rastinejad, F. (2001). Physical Structure of Nuclear Receptor-DNA Complexes. In: Lieberman, B.A. (eds) Steroid Receptor Methods. Methods in Molecular Biology™, vol 176. Humana Press. https://doi.org/10.1385/1-59259-115-9:91
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DOI: https://doi.org/10.1385/1-59259-115-9:91
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