Structural and functional analysis of the N-terminal extracellular region of β-dystroglycan

被引:36
作者
Di Stasio, E [1 ]
Sciandra, F [1 ]
Maras, B [1 ]
Di Tommaso, F [1 ]
Petrucci, TC [1 ]
Giardina, B [1 ]
Brancaccio, A [1 ]
机构
[1] Univ Cattolica Sacro Cuore, Ist Chim & Chim Clin, Ctr Studio Chim Recettori & Mol Biologicamente At, CNR, I-00168 Rome, Italy
关键词
D O I
10.1006/bbrc.1999.1803
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 1999 Academic Press.
引用
收藏
页码:274 / 278
页数:5
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