1RXR

HIGH RESOLUTION SOLUTION STRUCTURE OF THE RETINOID X RECEPTOR DNA BINDING DOMAIN, NMR, 20 STRUCTURE

Summary for 1RXR

• Entry DOI: 10.2210/pdb1rxr/pdb
• NMR Information: BMRB: 4153
• Descriptor: RETINOIC ACID RECEPTOR-ALPHA, ZINC ION (2 entities in total)
• Functional Keywords: transcription factor, nuclear hormone receptor, zinc-finger
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : P19793
• Total number of polymer chains: 1
• Total formula weight: 9948.21

Authors

Holmbeck, S.M.A.,Foster, M.P.,Casimiro, D.R.,Sem, D.S.,Dyson, H.J.,Wright, P.E. (deposition date: 1998-06-12, release date: 1998-11-11, Last modification date: 2024-05-01)

Primary citation

Holmbeck, S.M.,Foster, M.P.,Casimiro, D.R.,Sem, D.S.,Dyson, H.J.,Wright, P.E.
High-resolution solution structure of the retinoid X receptor DNA-binding domain.
J.Mol.Biol., 281:271-284, 1998

PubMed Abstract: 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.

PubMed: 9698548
DOI: 10.1006/jmbi.1998.1908

Experimental method

SOLUTION NMR