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1R4I

Crystal Structure of Androgen Receptor DNA-Binding Domain Bound to a Direct Repeat Response Element

Summary for 1R4I
Entry DOI10.2210/pdb1r4i/pdb
Descriptor5'-D(*CP*CP*AP*GP*AP*AP*CP*AP*TP*CP*AP*AP*GP*AP*AP*CP*AP*G)-3', 5'-D(*CP*TP*GP*TP*TP*CP*TP*TP*GP*AP*TP*GP*TP*TP*CP*TP*GP*G)-3', Androgen receptor, ... (4 entities in total)
Functional Keywordsar, steroid receptor, protein-dna complex, androgen, transcription-dna complex, transcription/dna
Biological sourceRattus norvegicus (Norway rat)
Cellular locationNucleus: P15207
Total number of polymer chains4
Total formula weight34589.54
Authors
Shaffer, P.L.,Jivan, A.,Dollins, D.E.,Claessens, F.,Gewirth, D.T. (deposition date: 2003-10-06, release date: 2004-06-29, Last modification date: 2024-10-16)
Primary citationShaffer, P.L.,Jivan, A.,Dollins, D.E.,Claessens, F.,Gewirth, D.T.
Structural basis of androgen receptor binding to selective androgen response elements.
Proc.Natl.Acad.Sci.USA, 101:4758-4763, 2004
Cited by
PubMed Abstract: Steroid receptors bind as dimers to a degenerate set of response elements containing inverted repeats of a hexameric half-site separated by 3 bp of spacer (IR3). Naturally occurring selective androgen response elements have recently been identified that resemble direct repeats of the hexameric half-site (ADR3). The 3D crystal structure of the androgen receptor (AR) DNA-binding domain bound to a selective ADR3 reveals an unexpected head-to-head arrangement of the two protomers rather than the expected head-to-tail arrangement seen in nuclear receptors bound to response elements of similar geometry. Compared with the glucocorticoid receptor, the DNA-binding domain dimer interface of the AR has additional interactions that stabilize the AR dimer and increase the affinity for nonconsensus response elements. This increased interfacial stability compared with the other steroid receptors may account for the selective binding of AR to ADR3 response elements.
PubMed: 15037741
DOI: 10.1073/pnas.0401123101
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.1 Å)
Structure validation

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