2c7a: Difference between revisions

Revision as of 15:38, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2c7a.png

Template:STRUCTURE 2c7a

STRUCTURE OF THE PROGESTERONE RECEPTOR-DNA COMPLEXSTRUCTURE OF THE PROGESTERONE RECEPTOR-DNA COMPLEX

Template:ABSTRACT PUBMED 16931575

About this StructureAbout this Structure

2C7A is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Tue Jul 29 15:38:13 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''STRUCTURE OF THE PROGESTERONE RECEPTOR-DNA COMPLEX'''
+===STRUCTURE OF THE PROGESTERONE RECEPTOR-DNA COMPLEX===
-==Overview==
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-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.
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