1ynw: Difference between revisions

Revision as of 02:55, 28 July 2008

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File:1ynw.png

Template:STRUCTURE 1ynw

Crystal Structure of Vitmain D Receptor and 9-cis Retinoic Acid Receptor DNA-Binding Domains Bound to a DR3 Response ElementCrystal Structure of Vitmain D Receptor and 9-cis Retinoic Acid Receptor DNA-Binding Domains Bound to a DR3 Response Element

Template:ABSTRACT PUBMED 15225774

About this StructureAbout this Structure

1YNW is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structural analysis of RXR-VDR interactions on DR3 DNA., Shaffer PL, Gewirth DT, J Steroid Biochem Mol Biol. 2004 May;89-90(1-5):215-9. PMID:15225774

Page seeded by OCA on Mon Jul 28 02:55:35 2008

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OCA

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-'''Crystal Structure of Vitmain D Receptor and 9-cis Retinoic Acid Receptor DNA-Binding Domains Bound to a DR3 Response Element'''
+===Crystal Structure of Vitmain D Receptor and 9-cis Retinoic Acid Receptor DNA-Binding Domains Bound to a DR3 Response Element===
-==Overview==
+<!--
-The Vitamin D receptor (VDR) is a ligand-responsive transcription factor that forms homo- or heterodimers on response elements composed of two hexameric half-sites separated by three base pairs of spacer DNA. Binding of 1alpha,25-dihydroxyvitamin D(3) to the full-length VDR causes destabilization of the VDR homodimer and formation of a heterodimeric complex with the 9-cis retinoic acid receptor (RXR). VDR and RXR DNA-binding domains (DBDs) do not mimic this behavior, however: VDR DBD homodimers are formed exclusively, even in the presence of excess RXR DBD. Exploiting the asymmetry of the heterodimer and our knowledge of the homodimeric DBD interface, we have engineered VDR mutants that disfavor the homodimeric complex and allow for the formation of heterodimeric DBD complexes with RXR on DR3 elements. One of these complexes has been crystallized and its structure determined. However, the polarity of the proteins relative to the DNA is non-physiological due to crystal packing between symmetry-related VDR DBD protomers. This reveals a flattened energy landscape that appears to rely on elements outside of the core DBD for response element discrimination in the heterodimer.
+The line below this paragraph, {{ABSTRACT_PUBMED_15225774}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15225774 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15225774}}
 ==About this Structure==
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 [[Category: Rxr]]
 [[Category: Vdr]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 16:33:42 2008''
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