Structure of the retinoid X receptor a DNA binding domain: A helix required for homodimeric DNA binding

Min S. Lee, Steven A. Kliewer, Joan Provencal, Peter E. Wright, Ronald M. Evans

Research output: Contribution to journalArticle

227 Citations (Scopus)

Abstract

The three-dimensional solution structure of the DNA binding domain (DBD) of the retinoid X receptor a (RXRα) was determined by nuclear magnetic resonance spectroscopy. The two zinc fingers of the RXR DBD fold to form a single structural domain that consists of two perpendicularly oriented helices and that resembles the corresponding regions of the glucocorticoid and estrogen receptors (GR and ER, respectively). However, in contrast to the DBDs of the GR and ER, the RXR DBD contains an additional helix immediately after the second zinc finger. This third helix mediates both protein-protein and protein-DNA interactions required for cooperative, dimeric binding of the RXR DBD to DNA. Identification of the third helix in the RXR DBD thus defines a structural feature required for selective dimerization of the RXR on hormone response elements composed of half-sites (5′-AGGTCA-3′) arranged as tandem repeats.

Original languageEnglish (US)
Pages (from-to)1117-1121
Number of pages5
JournalScience
Volume260
Issue number5111
StatePublished - 1993

Fingerprint

Retinoid X Receptors
DNA
Zinc Fingers
Proteins
Tandem Repeat Sequences
Glucocorticoid Receptors
Dimerization
Response Elements
Estrogen Receptors
Magnetic Resonance Spectroscopy
Hormones

ASJC Scopus subject areas

  • General

Cite this

Lee, M. S., Kliewer, S. A., Provencal, J., Wright, P. E., & Evans, R. M. (1993). Structure of the retinoid X receptor a DNA binding domain: A helix required for homodimeric DNA binding. Science, 260(5111), 1117-1121.

Structure of the retinoid X receptor a DNA binding domain : A helix required for homodimeric DNA binding. / Lee, Min S.; Kliewer, Steven A.; Provencal, Joan; Wright, Peter E.; Evans, Ronald M.

In: Science, Vol. 260, No. 5111, 1993, p. 1117-1121.

Research output: Contribution to journalArticle

Lee, MS, Kliewer, SA, Provencal, J, Wright, PE & Evans, RM 1993, 'Structure of the retinoid X receptor a DNA binding domain: A helix required for homodimeric DNA binding', Science, vol. 260, no. 5111, pp. 1117-1121.
Lee, Min S. ; Kliewer, Steven A. ; Provencal, Joan ; Wright, Peter E. ; Evans, Ronald M. / Structure of the retinoid X receptor a DNA binding domain : A helix required for homodimeric DNA binding. In: Science. 1993 ; Vol. 260, No. 5111. pp. 1117-1121.
@article{35d4d6557a664fb481b9c010074e260a,
title = "Structure of the retinoid X receptor a DNA binding domain: A helix required for homodimeric DNA binding",
abstract = "The three-dimensional solution structure of the DNA binding domain (DBD) of the retinoid X receptor a (RXRα) was determined by nuclear magnetic resonance spectroscopy. The two zinc fingers of the RXR DBD fold to form a single structural domain that consists of two perpendicularly oriented helices and that resembles the corresponding regions of the glucocorticoid and estrogen receptors (GR and ER, respectively). However, in contrast to the DBDs of the GR and ER, the RXR DBD contains an additional helix immediately after the second zinc finger. This third helix mediates both protein-protein and protein-DNA interactions required for cooperative, dimeric binding of the RXR DBD to DNA. Identification of the third helix in the RXR DBD thus defines a structural feature required for selective dimerization of the RXR on hormone response elements composed of half-sites (5′-AGGTCA-3′) arranged as tandem repeats.",
author = "Lee, {Min S.} and Kliewer, {Steven A.} and Joan Provencal and Wright, {Peter E.} and Evans, {Ronald M.}",
year = "1993",
language = "English (US)",
volume = "260",
pages = "1117--1121",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5111",

}

TY - JOUR

T1 - Structure of the retinoid X receptor a DNA binding domain

T2 - A helix required for homodimeric DNA binding

AU - Lee, Min S.

AU - Kliewer, Steven A.

AU - Provencal, Joan

AU - Wright, Peter E.

AU - Evans, Ronald M.

PY - 1993

Y1 - 1993

N2 - The three-dimensional solution structure of the DNA binding domain (DBD) of the retinoid X receptor a (RXRα) was determined by nuclear magnetic resonance spectroscopy. The two zinc fingers of the RXR DBD fold to form a single structural domain that consists of two perpendicularly oriented helices and that resembles the corresponding regions of the glucocorticoid and estrogen receptors (GR and ER, respectively). However, in contrast to the DBDs of the GR and ER, the RXR DBD contains an additional helix immediately after the second zinc finger. This third helix mediates both protein-protein and protein-DNA interactions required for cooperative, dimeric binding of the RXR DBD to DNA. Identification of the third helix in the RXR DBD thus defines a structural feature required for selective dimerization of the RXR on hormone response elements composed of half-sites (5′-AGGTCA-3′) arranged as tandem repeats.

AB - The three-dimensional solution structure of the DNA binding domain (DBD) of the retinoid X receptor a (RXRα) was determined by nuclear magnetic resonance spectroscopy. The two zinc fingers of the RXR DBD fold to form a single structural domain that consists of two perpendicularly oriented helices and that resembles the corresponding regions of the glucocorticoid and estrogen receptors (GR and ER, respectively). However, in contrast to the DBDs of the GR and ER, the RXR DBD contains an additional helix immediately after the second zinc finger. This third helix mediates both protein-protein and protein-DNA interactions required for cooperative, dimeric binding of the RXR DBD to DNA. Identification of the third helix in the RXR DBD thus defines a structural feature required for selective dimerization of the RXR on hormone response elements composed of half-sites (5′-AGGTCA-3′) arranged as tandem repeats.

UR - http://www.scopus.com/inward/record.url?scp=0027222793&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027222793&partnerID=8YFLogxK

M3 - Article

C2 - 8388124

AN - SCOPUS:0027222793

VL - 260

SP - 1117

EP - 1121

JO - Science

JF - Science

SN - 0036-8075

IS - 5111

ER -