Summary information and primary citation
- PDB-id
-
2c7a;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- receptor-DNA
- Method
- X-ray (2.5 Å)
- Summary
- Structure of the progesterone receptor-DNA complex
- Reference
-
Roemer SC, Donham DC, Sherman L, Pon VH, Edwards DP,
Churchill MEA (2006): "Structure
of the Progesterone Receptor-Deoxyribonucleic Acid
Complex: Novel Interactions Required for Binding to
Half-Site Response Elements."
Mol.Endocrinol., 20, 3042. doi:
10.1210/ME.2005-0511.
- 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.