The glucocorticoid receptor dimer interface allosterically transmits sequence-specific DNA signals-Reference-Cited by-同舟云学术

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The glucocorticoid receptor dimer interface allosterically transmits sequence-specific DNA signals

Published:2013-06-02 Issue:7 Volume:20 Page:876-883
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Watson Lisa C,Kuchenbecker Kristopher M,Schiller Benjamin J,Gross John D,Pufall Miles A,Yamamoto Keith R

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.2595.pdf

Reference59 articles.

1. Yamamoto, K.R., Darimont, B., Wagner, R. & Iniguez-Lluhi, J. Building transcriptional regulatory complexes: signals and surfaces. Cold Spring Harb. Symp. Quant. Biol. 63, 587–598 (1998).

2. Rosenfeld, M.G., Lunyak, V.V. & Glass, C.K. Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response. Genes Dev. 20, 1405–1428 (2006).

3. Ricketson, D., Hostick, U., Fang, L., Yamamoto, K. & Darimont, B. A conformational switch in the ligand-binding domain regulates the dependence of the glucocorticoid receptor on Hsp90. J. Mol. Biol. 368, 729–741 (2007).

4. Garza, A.M.S., Khan, S.H. & Kumar, R. Site-specific phosphorylation induces functionally active conformation in the intrinsically disordered N-terminal activation function (AF1) domain of the glucocorticoid receptor. Mol. Cell Biol. 30, 220–230 (2010).

5. Bledsoe, R.K. et al. Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition. Cell 110, 93–105 (2002).

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