Helical propensity in an intrinsically disordered protein accelerates ligand binding

Research output: Contribution to journal › Journal article › Research › peer-review

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Helical propensity in an intrinsically disordered protein accelerates ligand binding. / Iesmantavicius, Vytautas; Dogan, Jakob; Jemth, Per; Teilum, Kaare; Kjærgaard, Magnus.

In: Angewandte Chemie (International ed. in English), Vol. 53, No. 6, 2014, p. 1548-1551.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Iesmantavicius, V, Dogan, J, Jemth, P, Teilum, K & Kjærgaard, M 2014, 'Helical propensity in an intrinsically disordered protein accelerates ligand binding', Angewandte Chemie (International ed. in English), vol. 53, no. 6, pp. 1548-1551. https://doi.org/10.1002/anie.201307712

APA

Iesmantavicius, V., Dogan, J., Jemth, P., Teilum, K., & Kjærgaard, M. (2014). Helical propensity in an intrinsically disordered protein accelerates ligand binding. Angewandte Chemie (International ed. in English), 53(6), 1548-1551. https://doi.org/10.1002/anie.201307712

Vancouver

Iesmantavicius V, Dogan J, Jemth P, Teilum K, Kjærgaard M. Helical propensity in an intrinsically disordered protein accelerates ligand binding. Angewandte Chemie (International ed. in English). 2014;53(6):1548-1551. https://doi.org/10.1002/anie.201307712

Author

Iesmantavicius, Vytautas ; Dogan, Jakob ; Jemth, Per ; Teilum, Kaare ; Kjærgaard, Magnus. / Helical propensity in an intrinsically disordered protein accelerates ligand binding. In: Angewandte Chemie (International ed. in English). 2014 ; Vol. 53, No. 6. pp. 1548-1551.

Bibtex

@article{fd0095f2bf524a15a14c33b52464d1d5,

title = "Helical propensity in an intrinsically disordered protein accelerates ligand binding",

abstract = "Many intrinsically disordered proteins fold upon binding to other macromolecules. The secondary structure present in the well-ordered complex is often formed transiently in the unbound state. The consequence of such transient structure for the binding process is, however, not clear. The activation domain of the activator for thyroid hormone and retinoid receptors (ACTR) is intrinsically disordered and folds upon binding to the nuclear coactivator binding domain (NCBD) of the CREB binding protein. A number of mutants was designed that selectively perturbs the amount of secondary structure in unbound ACTR without interfering with the intermolecular interactions between ACTR and NCBD. Using NMR spectroscopy and fluorescence-monitored stopped-flow kinetic measurements we show that the secondary structure content in helix 1 of ACTR indeed influences the binding kinetics. The results thus support the notion of preformed secondary structure as an important determinant for molecular recognition in intrinsically disordered proteins.",

author = "Vytautas Iesmantavicius and Jakob Dogan and Per Jemth and Kaare Teilum and Magnus Kj{\ae}rgaard",

note = "Copyright {\textcopyright} 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.",

year = "2014",

doi = "10.1002/anie.201307712",

language = "English",

volume = "53",

pages = "1548--1551",

journal = "Angewandte Chemie International Edition",

issn = "1433-7851",

publisher = "Wiley-VCH Verlag GmbH & Co. KGaA",

number = "6",

}

RIS

TY - JOUR

T1 - Helical propensity in an intrinsically disordered protein accelerates ligand binding

AU - Iesmantavicius, Vytautas

AU - Dogan, Jakob

AU - Jemth, Per

AU - Teilum, Kaare

AU - Kjærgaard, Magnus

PY - 2014

Y1 - 2014

N2 - Many intrinsically disordered proteins fold upon binding to other macromolecules. The secondary structure present in the well-ordered complex is often formed transiently in the unbound state. The consequence of such transient structure for the binding process is, however, not clear. The activation domain of the activator for thyroid hormone and retinoid receptors (ACTR) is intrinsically disordered and folds upon binding to the nuclear coactivator binding domain (NCBD) of the CREB binding protein. A number of mutants was designed that selectively perturbs the amount of secondary structure in unbound ACTR without interfering with the intermolecular interactions between ACTR and NCBD. Using NMR spectroscopy and fluorescence-monitored stopped-flow kinetic measurements we show that the secondary structure content in helix 1 of ACTR indeed influences the binding kinetics. The results thus support the notion of preformed secondary structure as an important determinant for molecular recognition in intrinsically disordered proteins.

AB - Many intrinsically disordered proteins fold upon binding to other macromolecules. The secondary structure present in the well-ordered complex is often formed transiently in the unbound state. The consequence of such transient structure for the binding process is, however, not clear. The activation domain of the activator for thyroid hormone and retinoid receptors (ACTR) is intrinsically disordered and folds upon binding to the nuclear coactivator binding domain (NCBD) of the CREB binding protein. A number of mutants was designed that selectively perturbs the amount of secondary structure in unbound ACTR without interfering with the intermolecular interactions between ACTR and NCBD. Using NMR spectroscopy and fluorescence-monitored stopped-flow kinetic measurements we show that the secondary structure content in helix 1 of ACTR indeed influences the binding kinetics. The results thus support the notion of preformed secondary structure as an important determinant for molecular recognition in intrinsically disordered proteins.

U2 - 10.1002/anie.201307712

DO - 10.1002/anie.201307712

M3 - Journal article

C2 - 24449148

VL - 53

SP - 1548

EP - 1551

JO - Angewandte Chemie International Edition

JF - Angewandte Chemie International Edition

SN - 1433-7851

IS - 6

ER -

ID: 109551772

Forskning