期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 78, 期 16, 页码 3409-3427出版社
WILEY
DOI: 10.1002/prot.22848
关键词
laminin; N-terminal domains; disulfide bonds; chemical cross-linking; mass spectrometry; computational modeling
资金
- Deutsche Forschungsgemeinschaft (DFG) [SI 867/7-1, SM 65/1-3, Graduiertenkolleg 1026]
- Medical Faculty of the University of Cologne
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 beta(1) and gamma(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 beta(1) and gamma(1) LN domains share the galactose-binding domain-like fold.
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