Laminin G-like domains: dystroglycan-specific lectins.

ABSTRACT: A unique O-mannose-linked glycan on the transmembrane protein dystroglycan binds a number of extracellular matrix proteins containing laminin G-like (LG) domains. The dystroglycan-matrix interaction is essential for muscle function: disrupted biosynthesis of the matrix-binding modification causes several forms of muscular dystrophy. The complete chemical structure of this modification has been deciphered in the past few years. We now know that LG domains bind to a glycosaminoglycan-like polysaccharide of [-3GlcAβ1,3Xylα1-] units, termed matriglycan, that is attached to a highly unusual heptasaccharide linker. X-ray crystallography has revealed the principles of Ca²⁺-dependent matriglycan binding by LG domains. In this review, the new structural insights are applied to the growin

SUBMITTER: Hohenester E 

PROVIDER: S-EPMC6925595 | biostudies-literature | 2019 Jun

REPOSITORIES: biostudies-literature