Probing the stability of the “naked” mucin-like domain of human α-dystroglycan

Abstract

α-Dystroglycan (α-DG) is heavily glycosylated within its central mucin-like domain. The glycosylation shell of α-dystroglycan is known to largely influence its functional properties toward extracellular ligands. The structural features of this α-dystroglycan domain have been poorly studied so far. For the first time, we have attempted a recombinant… (More)
DOI: 10.1186/1471-2091-14-15

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