Laminin G-like domains: dystroglycan-specific lectins.


Journal

Current opinion in structural biology
ISSN: 1879-033X
Titre abrégé: Curr Opin Struct Biol
Pays: England
ID NLM: 9107784

Informations de publication

Date de publication:
06 2019
Historique:
received: 21 08 2018
revised: 23 11 2018
accepted: 23 11 2018
pubmed: 12 12 2018
medline: 9 6 2020
entrez: 12 12 2018
Statut: ppublish

Résumé

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 Ca

Identifiants

pubmed: 30530204
pii: S0959-440X(18)30098-8
doi: 10.1016/j.sbi.2018.11.007
pmc: PMC6925595
mid: EMS85259
pii:
doi:

Substances chimiques

Laminin 0
Lectins 0
Dystroglycans 146888-27-9

Types de publication

Journal Article Research Support, Non-U.S. Gov't Review

Langues

eng

Sous-ensembles de citation

IM

Pagination

56-63

Subventions

Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 101748/Z/13/Z
Pays : United Kingdom

Informations de copyright

Copyright © 2018 Elsevier Ltd. All rights reserved.

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Auteurs

Erhard Hohenester (E)

Department of Life Sciences, Imperial College London, London SW7 2AZ, United Kingdom. Electronic address: e.hohenester@imperial.ac.uk.

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Classifications MeSH