Photo-CIDNP study of the interaction between the glucocorticoid receptor DNA-binding domain and glucocorticoid response elements.

E. Kellenbach; T. Härd; R. Boelens; K. Dahlman; J. Carlstedt-Duke; J.A. Gustafsson; G.A. van der Marel; J.H. van Boom; B. Maler; K.R. Yamamoto

Photo-CIDNP study of the interaction between the glucocorticoid receptor DNA-binding domain and glucocorticoid response elements.

E. Kellenbach
, T. Härd
, R. Boelens
, K. Dahlman
, J. Carlstedt-Duke
, J.A. Gustafsson
, G.A. van der Marel
, J.H. van Boom
, B. Maler
, K.R. Yamamoto

Research output: Contribution to journal › Article › Academic › peer-review

Abstract

Photo-CIDNP studies were performed on two protein fragments that both contain the double zinc-finger DNA-binding domain of the glucocorticoid receptor. In the absence of DNA, Tyr452 and Tyr474 are polarised in both fragments while Tyr497 is not. Addition of a palindromic glucocorticoid response element (GRE) results in the suppression of Tyr474 polarization while the polarization of Tyr452 is unaffected. The same result is observed upon adding a half GRE to the protein fragment indicating that the suppression of Tyr474 polarization is not due to protein-protein contacts but to interaction with DNA.

Original language	English
Pages (from-to)	105-110
Number of pages	6
Journal	Journal of Biomolecular NMR
Volume	1
Issue number	1
Publication status	Published - 1 May 1991

Keywords

coloring agent
DNA
DNA binding protein
glucocorticoid receptor
peptide fragment
zinc finger protein
amino acid sequence
animal
article
binding site
conformation
metabolism
methodology
molecular genetics
nuclear magnetic resonance spectroscopy
nucleotide sequence
photochemistry
protein binding
protein conformation
radiation exposure
rat
regulatory sequence

Cite this

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title = "Photo-CIDNP study of the interaction between the glucocorticoid receptor DNA-binding domain and glucocorticoid response elements.",

abstract = "Photo-CIDNP studies were performed on two protein fragments that both contain the double zinc-finger DNA-binding domain of the glucocorticoid receptor. In the absence of DNA, Tyr452 and Tyr474 are polarised in both fragments while Tyr497 is not. Addition of a palindromic glucocorticoid response element (GRE) results in the suppression of Tyr474 polarization while the polarization of Tyr452 is unaffected. The same result is observed upon adding a half GRE to the protein fragment indicating that the suppression of Tyr474 polarization is not due to protein-protein contacts but to interaction with DNA.",

keywords = "coloring agent, DNA, DNA binding protein, glucocorticoid receptor, peptide fragment, zinc finger protein, amino acid sequence, animal, article, binding site, conformation, metabolism, methodology, molecular genetics, nuclear magnetic resonance spectroscopy, nucleotide sequence, photochemistry, protein binding, protein conformation, radiation exposure, rat, regulatory sequence",

author = "E. Kellenbach and T. H{\"a}rd and R. Boelens and K. Dahlman and J. Carlstedt-Duke and J.A. Gustafsson and \{van der Marel\}, G.A. and \{van Boom\}, J.H. and B. Maler and K.R. Yamamoto",

year = "1991",

month = may,

day = "1",

language = "English",

volume = "1",

pages = "105--110",

journal = "Journal of Biomolecular NMR",

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TY - JOUR

T1 - Photo-CIDNP study of the interaction between the glucocorticoid receptor DNA-binding domain and glucocorticoid response elements.

AU - Kellenbach, E.

AU - Härd, T.

AU - Boelens, R.

AU - Dahlman, K.

AU - Carlstedt-Duke, J.

AU - Gustafsson, J.A.

AU - van der Marel, G.A.

AU - van Boom, J.H.

AU - Maler, B.

AU - Yamamoto, K.R.

PY - 1991/5/1

Y1 - 1991/5/1

N2 - Photo-CIDNP studies were performed on two protein fragments that both contain the double zinc-finger DNA-binding domain of the glucocorticoid receptor. In the absence of DNA, Tyr452 and Tyr474 are polarised in both fragments while Tyr497 is not. Addition of a palindromic glucocorticoid response element (GRE) results in the suppression of Tyr474 polarization while the polarization of Tyr452 is unaffected. The same result is observed upon adding a half GRE to the protein fragment indicating that the suppression of Tyr474 polarization is not due to protein-protein contacts but to interaction with DNA.

AB - Photo-CIDNP studies were performed on two protein fragments that both contain the double zinc-finger DNA-binding domain of the glucocorticoid receptor. In the absence of DNA, Tyr452 and Tyr474 are polarised in both fragments while Tyr497 is not. Addition of a palindromic glucocorticoid response element (GRE) results in the suppression of Tyr474 polarization while the polarization of Tyr452 is unaffected. The same result is observed upon adding a half GRE to the protein fragment indicating that the suppression of Tyr474 polarization is not due to protein-protein contacts but to interaction with DNA.

KW - coloring agent

KW - DNA

KW - DNA binding protein

KW - glucocorticoid receptor

KW - peptide fragment

KW - zinc finger protein

KW - amino acid sequence

KW - animal

KW - article

KW - binding site

KW - conformation

KW - metabolism

KW - methodology

KW - molecular genetics

KW - nuclear magnetic resonance spectroscopy

KW - nucleotide sequence

KW - photochemistry

KW - protein binding

KW - protein conformation

KW - radiation exposure

KW - rat

KW - regulatory sequence

M3 - Article

SN - 0925-2738

VL - 1

SP - 105

EP - 110

JO - Journal of Biomolecular NMR

JF - Journal of Biomolecular NMR

IS - 1

ER -

Photo-CIDNP study of the interaction between the glucocorticoid receptor DNA-binding domain and glucocorticoid response elements.

Abstract

Keywords

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