2C7A
STRUCTURE OF THE PROGESTERONE RECEPTOR-DNA COMPLEX
Summary for 2C7A
Entry DOI | 10.2210/pdb2c7a/pdb |
Related | 1A28 1E3K 1SQN 1SR7 1ZUC |
Descriptor | PROGESTERONE RECEPTOR, 5'-D(*CP*CP*AP*GP*AP*AP*CP*AP*GP*TP *TP*TP*GP*TP*TP*CP*TP*G)-3', 5'-D(*CP*CP*AP*GP*AP*AP*CP*AP*AP*AP *CP*TP*GP*TP*TP*CP*TP*G)-3', ... (5 entities in total) |
Functional Keywords | receptor/dna, progesterone receptor, dna-binding, complex, metal-binding, nuclear protein, phosphorylation, steroid-binding, transcription regulation, zinc-finger, zinc, receptor-dna complex |
Biological source | HOMO SAPIENS (HUMAN) More |
Cellular location | Nucleus. Isoform A: Nucleus: P06401 |
Total number of polymer chains | 4 |
Total formula weight | 28605.62 |
Authors | Roemer, S.C.,Donham, D.C.,Sherman, L.,Pon, V.H.,Edwards, D.P.,Churchill, M.E.A. (deposition date: 2005-11-19, release date: 2006-08-30, Last modification date: 2024-05-08) |
Primary citation | Roemer, S.C.,Donham, D.C.,Sherman, L.,Pon, V.H.,Edwards, D.P.,Churchill, M.E.A. Structure of the Progesterone Receptor-Deoxyribonucleic Acid Complex: Novel Interactions Required for Binding to Half-Site Response Elements. Mol.Endocrinol., 20:3042-, 2006 Cited by PubMed Abstract: 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. PubMed: 16931575DOI: 10.1210/ME.2005-0511 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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