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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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Abstract

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
Bibsysno:Link to catalogue
Publisher:Nature Publishing Co
ISSN:1072-8368
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:16 Apr 2019 15:54
Deposited On:22 Mar 2012 13:20

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