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Structural and Functional Analysis of the N-Terminal Extracellular Region of β-Dystroglycan

Biochemical and Biophysical Research Communications, ISSN: 0006-291X, Vol: 266, Issue: 1, Page: 274-278
1999
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Article Description

A protein fragment corresponding to the mouse β-dystroglycan N-terminal extracellular region from position 654 to 750, β-DG(654–750) was recombinantly expressed in BL21(DE3) Escherichia coli cells. Secondary structure prediction of the protein fragment reveals about 70% of random coil, as confirmed by circular dichroism analysis. Moreover, fluorescence analysis shows that the tryptophan residue in position 659 lays in a solvent-exposed fashion. These data suggest that the β-DG(654–750) is likely to have a quite flexible structure and to be only partially folded. Interestingly, the protein still retains its biological function since using solid-phase assays we have detected binding of biotinylated β-DG(654–750) both to native α-dystroglycan and to a recombinant fragment which spans the C-terminal region of α-dystroglycan.

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