Probing the stability of the "naked" mucin-like domain of human alpha-dystroglycan

Background: alpha-Dystroglycan (alpha-DG) is heavily glycosylated within its central mucin-like domain. The glycosylation shell of alpha-dystroglycan is known to largely influence its functional properties toward extracellular ligands. The structural features of this alpha-dystroglycan domain have been poorly studied so far. For the first time, we have attempted a recombinant expression approach in E. coli cells, in order to analyze by biochemical and biophysical techniques this important domain of the alpha-dystroglycan core protein.