Evolutionary fine-tuning of residual helix structure in disordered proteins manifests in complex structure and lifetime

Steffie Elkjær; Amanda D. Due; Lise F. Christensen; Frederik F. Theisen; Lasse Staby; Birthe B. Kragelund; Karen Skriver

doi:10.1038/s42003-023-04445-6

Communications Biology (Jan 2023)

Evolutionary fine-tuning of residual helix structure in disordered proteins manifests in complex structure and lifetime

Steffie Elkjær,
Amanda D. Due,
Lise F. Christensen,
Frederik F. Theisen,
Lasse Staby,
Birthe B. Kragelund,
Karen Skriver

Affiliations

Steffie Elkjær: The REPIN and The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen
Amanda D. Due: The REPIN and The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen
Lise F. Christensen: The REPIN and The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen
Frederik F. Theisen: The REPIN and The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen
Lasse Staby: The REPIN and The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen
Birthe B. Kragelund: The REPIN and The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen
Karen Skriver: The REPIN and The Linderstrøm-Lang Centre for Protein Science, Department of Biology, University of Copenhagen

DOI: https://doi.org/10.1038/s42003-023-04445-6
Journal volume & issue: Vol. 6, no. 1
pp. 1 – 11

Abstract

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Evolution-guided mutagenesis and biophysical analysis reveal that residual helical structure in the binding region of an intrinsically disordered protein regulates the lifetime of its complex by affecting its dissociation.

Published in Communications Biology

ISSN: 2399-3642 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science: Biology (General)
Website: https://www.nature.com/commsbio/

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