Structural biology of laminins.
cell adhesion
crystallography
extracellular matrix
Journal
Essays in biochemistry
ISSN: 1744-1358
Titre abrégé: Essays Biochem
Pays: England
ID NLM: 0043306
Informations de publication
Date de publication:
13 09 2019
13 09 2019
Historique:
received:
05
04
2019
revised:
26
04
2019
accepted:
30
04
2019
pubmed:
17
5
2019
medline:
23
5
2020
entrez:
17
5
2019
Statut:
epublish
Résumé
Laminins are large cell-adhesive glycoproteins that are required for the formation and function of basement membranes in all animals. Structural studies by electron microscopy in the early 1980s revealed a cross-shaped molecule, which subsequently was shown to consist of three distinct polypeptide chains. Crystallographic studies since the mid-1990s have added atomic detail to all parts of the laminin heterotrimer. The three short arms of the cross are made up of continuous arrays of disulphide-rich domains. The globular domains at the tips of the short arms mediate laminin polymerization; the surface regions involved in this process have been identified by structure-based mutagenesis. The long arm of the cross is an α-helical coiled coil of all three chains, terminating in a cell-adhesive globular region. The molecular basis of cell adhesion to laminins has been revealed by recent structures of heterotrimeric integrin-binding fragments and of a laminin fragment bound to the carbohydrate modification of dystroglycan. The structural characterization of the laminin molecule is essentially complete, but we still have to find ways of imaging native laminin polymers at molecular resolution.
Identifiants
pubmed: 31092689
pii: EBC20180075
doi: 10.1042/EBC20180075
pmc: PMC6744579
doi:
Substances chimiques
Integrins
0
Laminin
0
Membrane Glycoproteins
0
nidogen
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
285-295Subventions
Organisme : Wellcome Trust
Pays : United Kingdom
Informations de copyright
© 2019 The Author(s).
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