The laminin-binding domain of agrin is structurally related to N-TIMP-1

Stetefeld, J. and Jenny, M. and Schulthess, T. and Landwehr, R. and Schumacher, B. and Frank, S. and Ruegg, M. A. and Engel, J. and Kammerer, R. A.. (2001) The laminin-binding domain of agrin is structurally related to N-TIMP-1. Nature Structural biology, Vol. 8, H. 8. pp. 705-709.

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Agrin is the key organizer of postsynaptic differentiation at the neuromuscular junction. This organization activity requires the binding of agrin to the synaptic basal lamina. Binding is conferred by the N-terminal agrin (NtA) domain, which mediates a high-affinity interaction with the coiled coil domain of laminins. Here, we report the crystal structure of chicken NtA at 1.6 A resolution. The structure reveals that NtA harbors an oligosaccharide/oligonucleotide-binding fold with several possible sites for the interaction with different ligands. A high structural similarity of NtA with the protease inhibition domain in tissue inhibitor of metalloproteinases-1 (TIMP-1) supports the idea of additional functions of agrin besides synaptogenic activity.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Neurobiology > Pharmacology/Neurobiology (Rüegg)
UniBasel Contributors:Rüegg, Markus A.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Nature Publishing Co
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:16 Apr 2019 15:54
Deposited On:22 Mar 2012 13:20

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