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

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1999年 / 266卷 / 01期

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

页码：274 / 278

页数：5

共 37 条

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