1JC7
The Laminin-Binding Domain of Agrin is Structurally Related to N-TIMP-1
Summary for 1JC7
| Entry DOI | 10.2210/pdb1jc7/pdb |
| Related | 1JB3 |
| Descriptor | Agrin, CHLORIDE ION (2 entities in total) |
| Functional Keywords | neuromuscular junction, agrin, interaction coiled-doil proteins with globular proteins, ob-fold, timp, cell adhesion |
| Biological source | Gallus gallus (chicken) |
| Total number of polymer chains | 1 |
| Total formula weight | 15182.80 |
| Authors | Stetefeld, J. (deposition date: 2001-06-08, release date: 2001-08-08, Last modification date: 2024-10-30) |
| Primary citation | Stetefeld, J.,Jenny, M.,Schulthess, T.,Landwehr, R.,Schumacher, B.,Frank, S.,Ruegg, M.A.,Engel, J.,Kammerer, R.A. The laminin-binding domain of agrin is structurally related to N-TIMP-1. Nat.Struct.Biol., 8:705-709, 2001 Cited by PubMed 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. PubMed: 11473262DOI: 10.1038/90422 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.73 Å) |
Structure validation
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