1rxr
From Proteopedia
(New page: 200px<br /> <applet load="1rxr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rxr" /> '''HIGH RESOLUTION SOLUTION STRUCTURE OF THE R...) |
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'''HIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE'''<br /> | '''HIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
- | 1RXR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1RXR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXR OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
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Revision as of 14:50, 15 February 2008
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HIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE
Overview
The retinoid X receptor (RXR) is a member of the nuclear hormone receptor, superfamily of transcriptional regulators and plays a central role in the, retinoid and, through its ability to heterodimerize with other nuclear, hormone receptors, non-steroid signaling pathways. The DNA-binding and, recognition functions of RXR are located in a conserved 83 amino acid, residue domain that recognizes the consensus sequence AGGTCA. In order to, provide a detailed picture of its structure, we have calculated a, high-resolution solution structure of the C195A RXRalpha DNA-binding, domain. Structures were calculated using 1131 distance and dihedral angle, constraints derived from 1H, 13C and 15N NMR spectra. The structures, reveal a perpendicularly packed, "loop-helix" fold similar to other, nuclear hormone receptor DNA-binding domains and confirm the existence of, the C-terminal helix, which was first observed in the low-resolution NMR, structure. The C-terminal helix is well formed and is stabilized by, packing interactions with residues in the hydrophobic core. The solution, structure of RXR is very similar to that determined by X-ray, crystallographic studies of the RXR-TR heterodimer complex with DNA, except that in the latter case no electron density was observed for, residues corresponding to the C-terminal helix. Other differences between, the X-ray and NMR structures occur in the second zinc-binding loop, which, is disordered in solution. Heteronuclear 15N NOE measurements suggest that, this loop has enhanced flexibility in the free protein.
About this Structure
1RXR is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
High-resolution solution structure of the retinoid X receptor DNA-binding domain., Holmbeck SM, Foster MP, Casimiro DR, Sem DS, Dyson HJ, Wright PE, J Mol Biol. 1998 Aug 14;281(2):271-84. PMID:9698548
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