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Title (Primary) Computational modeling of laminin N-terminal domains using sparse distance constraints from disulfide bonds and chemical cross-linking
Author Kalkhof, S.; Haehn, S.; Paulsson, M.; Smyth, N.; Meiler, J.; Sinz, A.;
Journal Proteins: Structure, Function, and Bioinformatics
Year 2010
Department PROTEOM;
Volume 78
Issue 16
Language englisch;
Keywords laminin; N-terminal domains; disulfide bonds; chemical cross-linking; mass spectrometry; computational modeling
Abstract Basement membranes are thin extracellular protein layers, which separate endothelial and epithelial cells from the underlying connecting tissue. The main non-collagenous 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 ß1 and ?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, i.e., disulfide bonds as well as chemical cross-links obtained from reactions with two amine-reactive cross-linkers. We predict that laminin ß1 and ?1 LN domains share the galactose-binding domain-like fold. Proteins 2010.
ID 10136
Persistent UFZ Identifier https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=10136
Kalkhof, S., Haehn, S., Paulsson, M., Smyth, N., Meiler, J., Sinz, A. (2010):
Computational modeling of laminin N-terminal domains using sparse distance constraints from disulfide bonds and chemical cross-linking
Proteins 78 (16), 3409 - 3427