1rxr
From Proteopedia
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'''HIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE''' | '''HIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE''' | ||
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[[Category: Sem, D S.]] | [[Category: Sem, D S.]] | ||
[[Category: Wright, P E.]] | [[Category: Wright, P E.]] | ||
| - | [[Category: | + | [[Category: Nuclear hormone receptor]] |
| - | [[Category: | + | [[Category: Transcription factor]] |
| - | [[Category: | + | [[Category: Zinc-finger]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 08:02:04 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 05:02, 3 May 2008
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 Sat May 3 08:02:04 2008
