1rxr
From Proteopedia
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| - | [[Image:1rxr.jpg|left|200px]] | + | [[Image:1rxr.jpg|left|200px]] |
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| - | '''HIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE''' | + | {{Structure |
| + | |PDB= 1rxr |SIZE=350|CAPTION= <scene name='initialview01'>1rxr</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''HIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RXR is a [ | + | 1RXR is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RXR OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9698548 9698548] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:57:40 2008'' |
Revision as of 11:57, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 13:57:40 2008
