PDBsum entry 1rxr

Transcription factor

PDB id: 1rxr

Contents

Protein chain

83 a.a. *

Metals

_ZN ×2

* Residue conservation analysis

PDB id:

1rxr

Name:

Transcription factor

Title:

High resolution solution structure of the retinoid x receptor DNA binding domain, nmr, 20 structure

Structure:

Retinoic acid receptor-alpha. Chain: a. Fragment: DNA-binding domain, 130-212. Synonym: rxr-alpha. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Cell_line: bl21. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.

NMR struc:

20 models

Authors:

S.M.A.Holmbeck,M.P.Foster,D.R.Casimiro,D.S.Sem,H.J.Dyson,P.E.Wright

Key ref:

S.M.Holmbeck et al. (1998). High-resolution solution structure of the retinoid X receptor DNA-binding domain. J Mol Biol, 281, 271-284. PubMed id: 9698548 DOI: 10.1006/jmbi.1998.1908

Date:

12-Jun-98 Release date: 11-Nov-98

Protein chain

P19793  (RXRA_HUMAN) -  Retinoic acid receptor RXR-alpha from Homo sapiens

Seq: 462 a.a.

Struc: 83 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1006/jmbi.1998.1908

J Mol Biol 281:271-284 (1998)

PubMed id: 9698548

High-resolution solution structure of the retinoid X receptor DNA-binding domain.

S.M.Holmbeck, M.P.Foster, D.R.Casimiro, D.S.Sem, H.J.Dyson, P.E.Wright.

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.

Selected figure(s)

Figure 1.
Figure 1. The sequence and zinc-coordination of the human RXRa DNA-binding domain (F130 to G212) with C195A mutation.

Figure 3.
Figure 3. Stereoview of superposition of 20 structures with lowest AMBER energies, residues Lys132 to Gln210. The structures are superimposed to minimize RMS differences of backbone atoms for residues Ile134 to Arg209. Zinc atoms are shown as pink spheres. Sulfur atoms from zinc-coordinating cysteine residues are shown in yellow.

The above figures are reprinted by permission from Elsevier: J Mol Biol (1998, 281, 271-284) copyright 1998.

Figures were selected by an automated process.