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

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 affe...

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Autores principales:	Adam W. Avery, Michael E. Fealey, Fengbin Wang, Albina Orlova, Andrew R. Thompson, David D. Thomas, Thomas S. Hays, Edward H. Egelman
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/31f88968062445619400ace9c16ea35b
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spelling	oai:doaj.org-article:31f88968062445619400ace9c16ea35b2021-12-02T17:06:26ZStructural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation10.1038/s41467-017-01367-w2041-1723https://doaj.org/article/31f88968062445619400ace9c16ea35b2017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01367-whttps://doaj.org/toc/2041-1723The 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.Adam W. AveryMichael E. FealeyFengbin WangAlbina OrlovaAndrew R. ThompsonDavid D. ThomasThomas S. HaysEdward H. EgelmanNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-7 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Adam W. Avery Michael E. Fealey Fengbin Wang Albina Orlova Andrew R. Thompson David D. Thomas Thomas S. Hays Edward H. Egelman Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation
description	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.
format	article
author	Adam W. Avery Michael E. Fealey Fengbin Wang Albina Orlova Andrew R. Thompson David D. Thomas Thomas S. Hays Edward H. Egelman
author_facet	Adam W. Avery Michael E. Fealey Fengbin Wang Albina Orlova Andrew R. Thompson David D. Thomas Thomas S. Hays Edward H. Egelman
author_sort	Adam W. Avery
title	Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation
title_short	Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation
title_full	Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation
title_fullStr	Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation
title_full_unstemmed	Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation
title_sort	structural basis for high-affinity actin binding revealed by a β-iii-spectrin sca5 missense mutation
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/31f88968062445619400ace9c16ea35b
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Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation

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