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International Union of Crystallography, Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 8(67), p. 871-876, 2011

DOI: 10.1107/s1744309111024249

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Structure of filamin A immunoglobulin-like repeat 10 fromHomo sapiens

Journal article published in 2011 by Richard C. Page ORCID, Jeffrey G. Clark, Saurav Misra
This paper is available in a repository.
This paper is available in a repository.

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Abstract

Filamin A (FlnA) plays a critical role in cytoskeletal organization, cell motility and cellular signaling. FlnA utilizes different binding sites on a series of 24 immunoglobulin-like domains (Ig repeats) to interact with diverse cytosolic proteins and with cytoplasmic portions of membrane proteins. Mutations in a specific domain, Ig10 (FlnA-Ig10), are correlated with two severe forms of the otopalatodigital syndrome spectrum disorders Melnick-Needles syndrome and frontometaphyseal dysplasia. The crystal structure of FlnA-Ig10 determined at 2.44 Å resolution provides insight into the perturbations caused by these mutations.