2c7a

STRUCTURE OF THE PROGESTERONE RECEPTOR-DNA COMPLEX

spinqualitylabelsall models 2c7a, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c7a is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Related: 1a28, 1e3k, 1sqn, 1sr7, 1zuc Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [PRGR_HUMAN] The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Progesterone receptor isoform B (PRB) is involved activation of c-SRC/MAPK signaling on hormone stimulation. Isoform A is inactive in stimulating c-Src/MAPK signaling on hormone stimulation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The DNA binding domain (DBD) of nuclear hormone receptors contains a highly conserved globular domain and a less conserved carboxyl-terminal extension (CTE). Despite previous observations that the CTEs of some classes of nuclear receptors are structured and interact with DNA outside of the hexanucleotide hormone response element (HRE), there has been no evidence for such a CTE among the steroid receptors. We have determined the structure of the progesterone receptor (PR)-DBD-CTE DNA complex at a resolution of 2.5 A, which revealed binding of the CTE to the minor groove flanking the HREs. Alanine substitutions of the interacting CTE residues reduced affinity for inverted repeat HREs separated by three nucleotides, and essentially abrogated binding to a single HRE. A highly compressed minor groove of the trinucleotide spacer and a novel dimerization interface were also observed. A PR binding site selection experiment revealed sequence preferences in the trinucleotide spacer and flanking DNA. These results, taken together, support the notion that sequences outside of the HREs influence the DNA binding affinity and specificity of steroid receptors. Structure of the progesterone receptor-deoxyribonucleic acid complex: novel interactions required for binding to half-site response elements.,Roemer SC, Donham DC, Sherman L, Pon VH, Edwards DP, Churchill ME Mol Endocrinol. 2006 Dec;20(12):3042-52. Epub 2006 Aug 24. PMID:16931575 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Progesterone receptor

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