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Cloning, expression, purification, crystallization and preliminary crystallographic analysis of -­filamin repeat 23

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Abstract:

Human -filamin is a protein of 2705 amino-acid residues that localizes mainly in the myofibrillar Z-disc and to smaller extent in the subsarcolemmal region of striated muscle cells. -Filamin consists of an N-terminal actin-binding domain followed by a long rod-shaped region. The rod-shaped region consists of 24 immunoglobulin-like domains that form a platform for interaction with different transmembrane, cell-signalling and cytoskeletal proteins. -Filamin repeat 23 was indicated as being necessary for binding to the muscle-specific subsarcolemmal proteins - and -sarcoglycan and the myofibrillar protein FATZ1. The recombinant -filamin repeat 23 was crystallized using the hanging-drop vapour-diffusion method, which yielded needle-shaped diffraction-quality crystals. Diffraction data were collected to 2.05 Å resolution using 1.2 Å wavelength synchrotron radiation. Preliminary structural analysis shows one molecule, with predominantly  secondary-structure elements, per asymmetric unit.

Keywords: FATZ; Ig-like domains; Z-disk; striated muscle; -filamin

Document Type: Research Article

DOI: https://doi.org/10.1107/S090744490400873X

Publication date: 2004-06-01

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