Ligand-specific conformational change drives interdomain allostery in Pin1

Alexandra Born; Janne Soetbeer; Morkos A. Henen; Frauke Breitgoff; Yevhen Polyhach; Gunnar Jeschke; Beat Vögeli

doi:10.1038/s41467-022-32340-x

Nature Communications (Aug 2022)

Ligand-specific conformational change drives interdomain allostery in Pin1

Alexandra Born,
Janne Soetbeer,
Morkos A. Henen,
Frauke Breitgoff,
Yevhen Polyhach,
Gunnar Jeschke,
Beat Vögeli

Affiliations

Alexandra Born: University of Colorado Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics
Janne Soetbeer: Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zürich, Vladimir-Prelog-Weg 2, ETH-Hönggerberg
Morkos A. Henen: University of Colorado Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics
Frauke Breitgoff: Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zürich, Vladimir-Prelog-Weg 2, ETH-Hönggerberg
Yevhen Polyhach: Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zürich, Vladimir-Prelog-Weg 2, ETH-Hönggerberg
Gunnar Jeschke: Laboratory of Physical Chemistry, Department of Chemistry and Applied Biosciences, ETH Zürich, Vladimir-Prelog-Weg 2, ETH-Hönggerberg
Beat Vögeli: University of Colorado Anschutz Medical Campus, Department of Biochemistry and Molecular Genetics

DOI: https://doi.org/10.1038/s41467-022-32340-x
Journal volume & issue: Vol. 13, no. 1
pp. 1 – 9

Abstract

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Born et al. describe interdomain allostery in the two domain peptidyl-prolyl isomerase Pin1 upon binding of two ligands. These ligands couple population shifts of extended and compact states to changes in the catalytic site of Pin1.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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