Extreme disorder in an ultrahigh-affinity protein complex

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Extreme disorder in an ultrahigh-affinity protein complex. / Borgia, Alessandro; Borgia, Madeleine B.; Bugge, Katrine Østergaard; Kissling, Vera M.; Heidarsson, Pétur O.; Fernandes, Catarina B.; Sottini, Andrea; Soranno, Andrea; Buholzer, Karin J.; Nettels, Daniel; Kragelund, Birthe Brandt; Best, Robert B.; Schuler, Benjamin.

I: Nature, Bind 555, 01.03.2018, s. 61-66.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Borgia, A, Borgia, MB, Bugge, KØ, Kissling, VM, Heidarsson, PO, Fernandes, CB, Sottini, A, Soranno, A, Buholzer, KJ, Nettels, D, Kragelund, BB, Best, RB & Schuler, B 2018, 'Extreme disorder in an ultrahigh-affinity protein complex', Nature, bind 555, s. 61-66. https://doi.org/10.1038/nature25762

APA

Borgia, A., Borgia, M. B., Bugge, K. Ø., Kissling, V. M., Heidarsson, P. O., Fernandes, C. B., Sottini, A., Soranno, A., Buholzer, K. J., Nettels, D., Kragelund, B. B., Best, R. B., & Schuler, B. (2018). Extreme disorder in an ultrahigh-affinity protein complex. Nature, 555, 61-66. https://doi.org/10.1038/nature25762

Vancouver

Borgia A, Borgia MB, Bugge KØ, Kissling VM, Heidarsson PO, Fernandes CB o.a. Extreme disorder in an ultrahigh-affinity protein complex. Nature. 2018 mar. 1;555:61-66. https://doi.org/10.1038/nature25762

Author

Borgia, Alessandro ; Borgia, Madeleine B. ; Bugge, Katrine Østergaard ; Kissling, Vera M. ; Heidarsson, Pétur O. ; Fernandes, Catarina B. ; Sottini, Andrea ; Soranno, Andrea ; Buholzer, Karin J. ; Nettels, Daniel ; Kragelund, Birthe Brandt ; Best, Robert B. ; Schuler, Benjamin. / Extreme disorder in an ultrahigh-affinity protein complex. I: Nature. 2018 ; Bind 555. s. 61-66.

Bibtex

@article{7a7adf3ff0d44f318bd538ec7dce62c9,
title = "Extreme disorder in an ultrahigh-affinity protein complex",
abstract = "Molecular communication in biology is mediated by protein interactions. According to the current paradigm, the specificity and affinity required for these interactions are encoded in the precise complementarity of binding interfaces. Even proteins that are disordered under physiological conditions or that contain large unstructured regions commonly interact with well-structured binding sites on other biomolecules. Here we demonstrate the existence of an unexpected interaction mechanism: the two intrinsically disordered human proteins histone H1 and its nuclear chaperone prothymosin-α associate in a complex with picomolar affinity, but fully retain their structural disorder, long-range flexibility and highly dynamic character. On the basis of closely integrated experiments and molecular simulations, we show that the interaction can be explained by the large opposite net charge of the two proteins, without requiring defined binding sites or interactions between specific individual residues. Proteome-wide sequence analysis suggests that this interaction mechanism may be abundant in eukaryotes.",
author = "Alessandro Borgia and Borgia, {Madeleine B.} and Bugge, {Katrine {\O}stergaard} and Kissling, {Vera M.} and Heidarsson, {P{\'e}tur O.} and Fernandes, {Catarina B.} and Andrea Sottini and Andrea Soranno and Buholzer, {Karin J.} and Daniel Nettels and Kragelund, {Birthe Brandt} and Best, {Robert B.} and Benjamin Schuler",
year = "2018",
month = mar,
day = "1",
doi = "10.1038/nature25762",
language = "English",
volume = "555",
pages = "61--66",
journal = "Nature",
issn = "0028-0836",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Extreme disorder in an ultrahigh-affinity protein complex

AU - Borgia, Alessandro

AU - Borgia, Madeleine B.

AU - Bugge, Katrine Østergaard

AU - Kissling, Vera M.

AU - Heidarsson, Pétur O.

AU - Fernandes, Catarina B.

AU - Sottini, Andrea

AU - Soranno, Andrea

AU - Buholzer, Karin J.

AU - Nettels, Daniel

AU - Kragelund, Birthe Brandt

AU - Best, Robert B.

AU - Schuler, Benjamin

PY - 2018/3/1

Y1 - 2018/3/1

N2 - Molecular communication in biology is mediated by protein interactions. According to the current paradigm, the specificity and affinity required for these interactions are encoded in the precise complementarity of binding interfaces. Even proteins that are disordered under physiological conditions or that contain large unstructured regions commonly interact with well-structured binding sites on other biomolecules. Here we demonstrate the existence of an unexpected interaction mechanism: the two intrinsically disordered human proteins histone H1 and its nuclear chaperone prothymosin-α associate in a complex with picomolar affinity, but fully retain their structural disorder, long-range flexibility and highly dynamic character. On the basis of closely integrated experiments and molecular simulations, we show that the interaction can be explained by the large opposite net charge of the two proteins, without requiring defined binding sites or interactions between specific individual residues. Proteome-wide sequence analysis suggests that this interaction mechanism may be abundant in eukaryotes.

AB - Molecular communication in biology is mediated by protein interactions. According to the current paradigm, the specificity and affinity required for these interactions are encoded in the precise complementarity of binding interfaces. Even proteins that are disordered under physiological conditions or that contain large unstructured regions commonly interact with well-structured binding sites on other biomolecules. Here we demonstrate the existence of an unexpected interaction mechanism: the two intrinsically disordered human proteins histone H1 and its nuclear chaperone prothymosin-α associate in a complex with picomolar affinity, but fully retain their structural disorder, long-range flexibility and highly dynamic character. On the basis of closely integrated experiments and molecular simulations, we show that the interaction can be explained by the large opposite net charge of the two proteins, without requiring defined binding sites or interactions between specific individual residues. Proteome-wide sequence analysis suggests that this interaction mechanism may be abundant in eukaryotes.

U2 - 10.1038/nature25762

DO - 10.1038/nature25762

M3 - Journal article

C2 - 29466338

VL - 555

SP - 61

EP - 66

JO - Nature

JF - Nature

SN - 0028-0836

ER -

ID: 190967961