1kb2
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(New page: 200px<br /> <applet load="1kb2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kb2, resolution 2.70Å" /> '''Crystal Structure o...)
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Revision as of 15:42, 12 November 2007
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Crystal Structure of VDR DNA-binding Domain Bound to Mouse Osteopontin (SPP) Response Element
Contents |
Overview
The vitamin D receptor (VDR) forms homo- or heterodimers on response, elements composed of two hexameric half-sites separated by 3 bp of spacer, DNA. We describe here the crystal structures at 2.7-2.8 A resolution of, the VDR DNA-binding region (DBD) in complex with response elements from, three different promoters: osteopontin (SPP), canonical DR3 and, osteocalcin (OC). These structures reveal the chemical basis for the, increased affinity of VDR for the SPP response element, and for the poor, stability of the VDR-OC complex, relative to the canonical DR3 response, element. The homodimeric protein-protein interface is stabilized by van, der Waals interactions and is predominantly non-polar. An extensive, alpha-helix at the C-terminal end of the VDR DBD resembles that found in, the thyroid hormone receptor (TR), and suggests a mechanism by which VDR, and TR discriminate among response elements. Selective structure-based, mutations in the asymmetric homodimeric interface result in a VDR DBD, protein that is defective in homodimerization but now forms heterodimers, with the 9-cis retinoic acid receptor (RXR) DBD.
Disease
Known diseases associated with this structure: Osteoporosis, involutional, 166710 (1) OMIM:[601769], Rickets, vitamin D-resistant, type IIA OMIM:[601769]
About this Structure
1KB2 is a Single protein structure of sequence from Homo sapiens with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis of VDR-DNA interactions on direct repeat response elements., Shaffer PL, Gewirth DT, EMBO J. 2002 May 1;21(9):2242-52. PMID:11980721
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