Structural and functional analysis of the N-terminal extracellular region of beta-dystroglycan |
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Authors: | Di Stasio E Sciandra F Maras B Di Tommaso F Petrucci T C Giardina B Brancaccio A |
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Institution: | Centro Chimica dei Recettori (CNR), Istituto di Chimica e Chimica Clinica, Università Cattolica del Sacro Cuore, L.go F. Vito 1, Rome, 00168, Italy. |
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Abstract: | A protein fragment corresponding to the mouse beta-dystroglycan N-terminal extracellular region from position 654 to 750, beta-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 beta-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 beta-DG(654-750) both to native alpha-dystroglycan and to a recombinant fragment which spans the C-terminal region of alpha-dystroglycan. |
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