1r4i
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(New page: 200px<br /> <applet load="1r4i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r4i, resolution 3.10Å" /> '''Crystal Structure o...)
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Revision as of 06:58, 18 November 2007
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Crystal Structure of Androgen Receptor DNA-Binding Domain Bound to a Direct Repeat Response Element
Overview
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.
About this Structure
1R4I is a Single protein structure of sequence from Rattus norvegicus with ZN as ligand. The following page contains interesting information on the relation of 1R4I with [Anabolic Steroids]. Full crystallographic information is available from OCA.
Reference
Structural basis of androgen receptor binding to selective androgen response elements., Shaffer PL, Jivan A, Dollins DE, Claessens F, Gewirth DT, Proc Natl Acad Sci U S A. 2004 Apr 6;101(14):4758-63. Epub 2004 Mar 22. PMID:15037741
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