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Structural and functional analysis of the N-terminal extracellular region of beta-dystroglycan.
- Source :
-
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1999 Dec 09; Vol. 266 (1), pp. 274-8. - Publication Year :
- 1999
-
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.<br /> (Copyright 1999 Academic Press.)
- Subjects :
- Amino Acid Sequence
Animals
Biotinylation
Circular Dichroism
Cytoskeletal Proteins genetics
Cytoskeletal Proteins isolation & purification
Disulfides chemistry
Disulfides metabolism
Dystroglycans
Escherichia coli genetics
Glycosylation
Ligands
Membrane Glycoproteins genetics
Membrane Glycoproteins isolation & purification
Mice
Molecular Sequence Data
Molecular Weight
Peptide Fragments genetics
Peptide Fragments isolation & purification
Protein Binding
Protein Folding
Protein Structure, Secondary
Protein Structure, Tertiary
Recombinant Proteins chemistry
Recombinant Proteins isolation & purification
Recombinant Proteins metabolism
Spectrometry, Fluorescence
Structure-Activity Relationship
Tryptophan chemistry
Tryptophan metabolism
Cytoskeletal Proteins chemistry
Cytoskeletal Proteins metabolism
Membrane Glycoproteins chemistry
Membrane Glycoproteins metabolism
Peptide Fragments chemistry
Peptide Fragments metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0006-291X
- Volume :
- 266
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Biochemical and biophysical research communications
- Publication Type :
- Academic Journal
- Accession number :
- 10581202
- Full Text :
- https://doi.org/10.1006/bbrc.1999.1803