The laminin-binding domain of agrin is structurally related to N-TIMP-1 |
| |
Authors: | Stetefeld J Jenny M Schulthess T Landwehr R Schumacher B Frank S Rüegg M A Engel J Kammerer R A |
| |
Affiliation: | Department of Biophysical Chemistry, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland. |
| |
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. |
| |
Keywords: | |
本文献已被 PubMed 等数据库收录! |
|