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
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Acceso en línea:https://doaj.org/article/31f88968062445619400ace9c16ea35b
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Sumario: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.