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Proteins. 2010 Dec;78(16):3409-27. doi: 10.1002/prot.22848. Epub 2010 Oct 11.

Computational modeling of laminin N-terminal domains using sparse distance constraints from disulfide bonds and chemical cross-linking.

Author information

1
Department of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin Luther University Halle-Wittenberg, Halle (Saale), Germany.

Abstract

Basement membranes are thin extracellular protein layers, which separate endothelial and epithelial cells from the underlying connecting tissue. The main noncollagenous components of basement membranes are laminins, trimeric glycoproteins, which form polymeric networks by interactions of their N-terminal (LN) domains; however, no high-resolution structure of laminin LN domains exists so far. To construct models for laminin β(1) and γ(1) LN domains, 14 potentially suited template structures were determined using fold recognition methods. For each target/template-combination comparative models were created with Rosetta. Final models were selected based on their agreement with experimentally obtained distance constraints from natural cross-links, that is, disulfide bonds as well as chemical cross-links obtained from reactions with two amine-reactive cross-linkers. We predict that laminin β(1) and γ(1) LN domains share the galactose-binding domain-like fold.

PMID:
20939100
PMCID:
PMC5079110
DOI:
10.1002/prot.22848
[Indexed for MEDLINE]
Free PMC Article

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