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Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

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Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation. / van Tilborg, P J; Mulder, Frans A. A.; de Backer, M M et al.
In: Biochemistry, Vol. 38, No. 7, 16.02.1999, p. 1951-1956.

Research output: Contribution to journal/Conference contribution in journal/Contribution to newspaper › Journal article › Research › peer-review

Harvard

van Tilborg, PJ, Mulder, FAA, de Backer, MM, Nair, M, van Heerde, EC, Folkers, G, van der Saag, PT, Karimi-Nejad, Y, Boelens, R & Kaptein, R 1999, 'Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation', Biochemistry, vol. 38, no. 7, pp. 1951-1956. https://doi.org/10.1021/bi982526q

APA

van Tilborg, P. J., Mulder, F. A. A., de Backer, M. M., Nair, M., van Heerde, E. C., Folkers, G., van der Saag, P. T., Karimi-Nejad, Y., Boelens, R., & Kaptein, R. (1999). Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation. Biochemistry, 38(7), 1951-1956. https://doi.org/10.1021/bi982526q

CBE

van Tilborg PJ, Mulder FAA, de Backer MM, Nair M, van Heerde EC, Folkers G, van der Saag PT, Karimi-Nejad Y, Boelens R, Kaptein R. 1999. Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation. Biochemistry. 38(7):1951-1956. https://doi.org/10.1021/bi982526q

MLA

van Tilborg, P J et al. "Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation". Biochemistry. 1999, 38(7). 1951-1956. https://doi.org/10.1021/bi982526q

Vancouver

van Tilborg PJ, Mulder FAA, de Backer MM, Nair M, van Heerde EC, Folkers G et al. Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation. Biochemistry. 1999 Feb 16;38(7):1951-1956. doi: 10.1021/bi982526q

Author

van Tilborg, P J ; Mulder, Frans A. A. ; de Backer, M M et al. / Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation. In: Biochemistry. 1999 ; Vol. 38, No. 7. pp. 1951-1956.

Bibtex

@article{9e253ef0ca4240d198993cead8c7ba05,
title = "Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation",
abstract = "The all-trans retinoic acid and 9-cis retinoic acid receptors (RAR and RXR, respectively) belong to a family of ligand inducible transcription factors, which exert their effect via binding to hormone response elements. Both are members of the class II sub-family of nuclear receptors, which bind DNA as dimers, on tandem repeats of a hexamer motif separated by a variable spacer. The variability in spacer length and the head-to-tail organization of the hormone response elements result in different protein-protein interactions in each of the complexes. We show that the zinc-coordinating loop regions of RXR and RAR DNA-binding domains exhibit dynamics on the millisecond to microsecond time scale. The highly dynamic second zinc finger of RXR constitutes the primary protein-protein interface in many nuclear receptor assemblies on DNA. Dynamics is also observed in the first and second zinc fingers of RAR, which are implicated in dimeric interactions with RXR on response elements with spacers of 5 base pairs and 1 base pair, respectively. The striking correspondence between the regions that exhibit conformational exchange and the dimer interfaces of the proteins complexed with DNA suggests a functional role for the dynamics. The observed flexibility may allow the proteins to adapt to various partners and with different orientations upon assembly on DNA. Furthermore, the more extensive dynamics observed for RXR may reflect the greater ability of this protein to modulate its interaction surface since it participates in a wide variety of receptor complexes.",
keywords = "Amino Acid Sequence, DNA, DNA-Binding Proteins, Dimerization, Humans, Macromolecular Substances, Models, Molecular, Molecular Sequence Data, Nuclear Magnetic Resonance, Biomolecular, Protein Structure, Tertiary, Receptors, Retinoic Acid, Retinoid X Receptors, Thermodynamics, Time Factors, Transcription Factors",
author = "{van Tilborg}, {P J} and Mulder, {Frans A. A.} and {de Backer}, {M M} and M Nair and {van Heerde}, {E C} and G Folkers and {van der Saag}, {P T} and Yasmin Karimi-Nejad and R Boelens and R Kaptein",
year = "1999",
month = feb,
day = "16",
doi = "10.1021/bi982526q",
language = "English",
volume = "38",
pages = "1951--1956",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "ACS Publications",
number = "7",

}

RIS

TY - JOUR

T1 - Millisecond to microsecond time scale dynamics of the retinoid X and retinoic acid receptor DNA-binding domains and dimeric complex formation

AU - van Tilborg, P J

AU - Mulder, Frans A. A.

AU - de Backer, M M

AU - Nair, M

AU - van Heerde, E C

AU - Folkers, G

AU - van der Saag, P T

AU - Karimi-Nejad, Yasmin

AU - Boelens, R

AU - Kaptein, R

PY - 1999/2/16

Y1 - 1999/2/16

N2 - The all-trans retinoic acid and 9-cis retinoic acid receptors (RAR and RXR, respectively) belong to a family of ligand inducible transcription factors, which exert their effect via binding to hormone response elements. Both are members of the class II sub-family of nuclear receptors, which bind DNA as dimers, on tandem repeats of a hexamer motif separated by a variable spacer. The variability in spacer length and the head-to-tail organization of the hormone response elements result in different protein-protein interactions in each of the complexes. We show that the zinc-coordinating loop regions of RXR and RAR DNA-binding domains exhibit dynamics on the millisecond to microsecond time scale. The highly dynamic second zinc finger of RXR constitutes the primary protein-protein interface in many nuclear receptor assemblies on DNA. Dynamics is also observed in the first and second zinc fingers of RAR, which are implicated in dimeric interactions with RXR on response elements with spacers of 5 base pairs and 1 base pair, respectively. The striking correspondence between the regions that exhibit conformational exchange and the dimer interfaces of the proteins complexed with DNA suggests a functional role for the dynamics. The observed flexibility may allow the proteins to adapt to various partners and with different orientations upon assembly on DNA. Furthermore, the more extensive dynamics observed for RXR may reflect the greater ability of this protein to modulate its interaction surface since it participates in a wide variety of receptor complexes.

AB - The all-trans retinoic acid and 9-cis retinoic acid receptors (RAR and RXR, respectively) belong to a family of ligand inducible transcription factors, which exert their effect via binding to hormone response elements. Both are members of the class II sub-family of nuclear receptors, which bind DNA as dimers, on tandem repeats of a hexamer motif separated by a variable spacer. The variability in spacer length and the head-to-tail organization of the hormone response elements result in different protein-protein interactions in each of the complexes. We show that the zinc-coordinating loop regions of RXR and RAR DNA-binding domains exhibit dynamics on the millisecond to microsecond time scale. The highly dynamic second zinc finger of RXR constitutes the primary protein-protein interface in many nuclear receptor assemblies on DNA. Dynamics is also observed in the first and second zinc fingers of RAR, which are implicated in dimeric interactions with RXR on response elements with spacers of 5 base pairs and 1 base pair, respectively. The striking correspondence between the regions that exhibit conformational exchange and the dimer interfaces of the proteins complexed with DNA suggests a functional role for the dynamics. The observed flexibility may allow the proteins to adapt to various partners and with different orientations upon assembly on DNA. Furthermore, the more extensive dynamics observed for RXR may reflect the greater ability of this protein to modulate its interaction surface since it participates in a wide variety of receptor complexes.

KW - Amino Acid Sequence

KW - DNA

KW - DNA-Binding Proteins

KW - Dimerization

KW - Humans

KW - Macromolecular Substances

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Protein Structure, Tertiary

KW - Receptors, Retinoic Acid

KW - Retinoid X Receptors

KW - Thermodynamics

KW - Time Factors

KW - Transcription Factors

U2 - 10.1021/bi982526q

DO - 10.1021/bi982526q

M3 - Journal article

C2 - 10026278

VL - 38

SP - 1951

EP - 1956

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 7

ER -