The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site.

The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site.

Dystroglycan (DG) is a membrane receptor, belonging to the dystrophin-glycoprotein complex (DGC) and formed by two subunits, α-dystroglycan (α-DG) and β-dystroglycan (β -DG). The C-terminal domain of α-DG and the N-terminal extracellular domain of β -DG are connected, providing a link between the ex...

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Main Authors: Magda Gioia, Giovanni Francesco Fasciglione, Diego Sbardella, Francesca Sciandra, MariaLuisa Casella, Serena Camerini, Marco Crescenzi, Alessandro Gori, Umberto Tarantino, Paola Cozza, Andrea Brancaccio, Massimo Coletta, Manuela Bozzi
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2018-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC5813964?pdf=render

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