Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation

Adam W. Avery; Michael E. Fealey; Fengbin Wang; Albina Orlova; Andrew R. Thompson; David D. Thomas; Thomas S. Hays; Edward H. Egelman

doi:10.1038/s41467-017-01367-w

Nature Communications (Nov 2017)

Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation

Adam W. Avery,
Michael E. Fealey,
Fengbin Wang,
Albina Orlova,
Andrew R. Thompson,
David D. Thomas,
Thomas S. Hays,
Edward H. Egelman

Affiliations

Adam W. Avery: Department of Genetics, Cell Biology and Development, University of Minnesota
Michael E. Fealey: Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota
Fengbin Wang: Department of Biochemistry and Molecular Genetics, University of Virginia
Albina Orlova: Department of Biochemistry and Molecular Genetics, University of Virginia
Andrew R. Thompson: Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota
David D. Thomas: Department of Biochemistry, Molecular Biology and Biophysics, University of Minnesota
Thomas S. Hays: Department of Genetics, Cell Biology and Development, University of Minnesota
Edward H. Egelman: Department of Biochemistry and Molecular Genetics, University of Virginia

DOI: https://doi.org/10.1038/s41467-017-01367-w
Journal volume & issue: Vol. 8, no. 1
pp. 1 – 7

Abstract

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The disease causing L253P mutation in the actin-binding domain (ABD) of β-III-spectrin drastically increases actin-binding affinity. Here, the authors present the cryo-EM structure of F-actin complexed with the ABD mutant and double electron–electron resonance measurements show how the mutation affects the ABD conformational state.

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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