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

Conclusions: Our analysis indirectly confirms the idea that the mucin-like domain of alpha-dystroglycan needs to be extensively glycosylated in order to reach a stable conformation. The absence/reduction of glycosylation by itself may greatly reduce the stability of the dystroglycan complex. Although an altered pattern of alpha-dystroglycan O-mannosylation, that is not significantly changing its overall glycosylation fraction, represents the primary molecular clue behind currently known dystroglycanopathies, it cannot be ruled out that still unidentified forms of alphaDG-related dystrophy might originate by a more substantial reduction of alpha-dystroglycan glycosylation and by its consequent destabilization.
Source: BMC Biochemistry - Category: Biochemistry Authors: Source Type: research