Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP

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Standard

Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. / Kjærgaard, Magnus; Teilum, Kaare; Poulsen, Flemming Martin.

I: Proceedings of the National Academy of Sciences of the United States of America, Bind 107, Nr. 28, 13.07.2010, s. 12535-40.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Kjærgaard, M, Teilum, K & Poulsen, FM 2010, 'Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP', Proceedings of the National Academy of Sciences of the United States of America, bind 107, nr. 28, s. 12535-40. https://doi.org/10.1073/pnas.1001693107

APA

Kjærgaard, M., Teilum, K., & Poulsen, F. M. (2010). Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. Proceedings of the National Academy of Sciences of the United States of America, 107(28), 12535-40. https://doi.org/10.1073/pnas.1001693107

CBE

Kjærgaard M, Teilum K, Poulsen FM. 2010. Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. Proceedings of the National Academy of Sciences of the United States of America. 107(28):12535-40. https://doi.org/10.1073/pnas.1001693107

MLA

Kjærgaard, Magnus, Kaare Teilum og Flemming Martin Poulsen. "Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP". Proceedings of the National Academy of Sciences of the United States of America. 2010, 107(28). 12535-40. https://doi.org/10.1073/pnas.1001693107

Vancouver

Kjærgaard M, Teilum K, Poulsen FM. Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. Proceedings of the National Academy of Sciences of the United States of America. 2010 jul 13;107(28):12535-40. https://doi.org/10.1073/pnas.1001693107

Author

Kjærgaard, Magnus ; Teilum, Kaare ; Poulsen, Flemming Martin. / Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP. I: Proceedings of the National Academy of Sciences of the United States of America. 2010 ; Bind 107, Nr. 28. s. 12535-40.

Bibtex

@article{18aed3eb720540428088e038d166eefc,
title = "Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP",
abstract = "Native molten globules are the most folded kind of intrinsically disordered proteins. Little is known about the mechanism by which native molten globules bind to their cognate ligands to form fully folded complexes. The nuclear coactivator binding domain (NCBD) of CREB binding protein is particularly interesting in this respect as structural studies of its complexes have shown that NCBD folds into two remarkably different states depending on the ligand being ACTR or IRF-3. The ligand-free state of NCBD was characterized in order to understand the mechanism of folding upon ligand binding. Biophysical studies show that despite the molten globule nature of the domain, it contains a small cooperatively folded core. By NMR spectroscopy, we have demonstrated that the folded core of NCBD has a well ordered conformer with specific side chain packing. This conformer resembles the structure of the NCBD in complex with the protein ligand, ACTR, suggesting that ACTR binds to prefolded NCBD molecules from the ensemble of interconverting structures.",
keywords = "Animals, CREB-Binding Protein, Ligands, Magnetic Resonance Spectroscopy, Mice, Molecular Conformation, Proteins",
author = "Magnus Kj{\ae}rgaard and Kaare Teilum and Poulsen, {Flemming Martin}",
year = "2010",
month = jul,
day = "13",
doi = "10.1073/pnas.1001693107",
language = "English",
volume = "107",
pages = "12535--40",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "28",

}

RIS

TY - JOUR

T1 - Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP

AU - Kjærgaard, Magnus

AU - Teilum, Kaare

AU - Poulsen, Flemming Martin

PY - 2010/7/13

Y1 - 2010/7/13

N2 - Native molten globules are the most folded kind of intrinsically disordered proteins. Little is known about the mechanism by which native molten globules bind to their cognate ligands to form fully folded complexes. The nuclear coactivator binding domain (NCBD) of CREB binding protein is particularly interesting in this respect as structural studies of its complexes have shown that NCBD folds into two remarkably different states depending on the ligand being ACTR or IRF-3. The ligand-free state of NCBD was characterized in order to understand the mechanism of folding upon ligand binding. Biophysical studies show that despite the molten globule nature of the domain, it contains a small cooperatively folded core. By NMR spectroscopy, we have demonstrated that the folded core of NCBD has a well ordered conformer with specific side chain packing. This conformer resembles the structure of the NCBD in complex with the protein ligand, ACTR, suggesting that ACTR binds to prefolded NCBD molecules from the ensemble of interconverting structures.

AB - Native molten globules are the most folded kind of intrinsically disordered proteins. Little is known about the mechanism by which native molten globules bind to their cognate ligands to form fully folded complexes. The nuclear coactivator binding domain (NCBD) of CREB binding protein is particularly interesting in this respect as structural studies of its complexes have shown that NCBD folds into two remarkably different states depending on the ligand being ACTR or IRF-3. The ligand-free state of NCBD was characterized in order to understand the mechanism of folding upon ligand binding. Biophysical studies show that despite the molten globule nature of the domain, it contains a small cooperatively folded core. By NMR spectroscopy, we have demonstrated that the folded core of NCBD has a well ordered conformer with specific side chain packing. This conformer resembles the structure of the NCBD in complex with the protein ligand, ACTR, suggesting that ACTR binds to prefolded NCBD molecules from the ensemble of interconverting structures.

KW - Animals

KW - CREB-Binding Protein

KW - Ligands

KW - Magnetic Resonance Spectroscopy

KW - Mice

KW - Molecular Conformation

KW - Proteins

U2 - 10.1073/pnas.1001693107

DO - 10.1073/pnas.1001693107

M3 - Journal article

C2 - 20616042

VL - 107

SP - 12535

EP - 12540

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 28

ER -