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Helical Propensity in an Intrinsically Disordered Protein Accelerates Ligand Binding
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Biochemistry and Microbiology.
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2014 (English)In: Angewandte Chemie International Edition, ISSN 1433-7851, E-ISSN 1521-3773, Vol. 53, no 6, 1548-1551 p.Article in journal (Refereed) Published
Abstract [en]

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 helix1 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.

Place, publisher, year, edition, pages
2014. Vol. 53, no 6, 1548-1551 p.
Keyword [en]
conformational selection, ligand binding, NMR spectroscopy, proteins, secondary structure
National Category
Natural Sciences
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URN: urn:nbn:se:uu:diva-220282DOI: 10.1002/anie.201307712ISI: 000330558400013OAI: oai:DiVA.org:uu-220282DiVA: diva2:706318
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De två första författarna delar första författarskapet.

Available from: 2014-03-19 Created: 2014-03-12 Last updated: 2017-12-05Bibliographically approved

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