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1JC7

The Laminin-Binding Domain of Agrin is Structurally Related to N-TIMP-1

Summary for 1JC7
Entry DOI10.2210/pdb1jc7/pdb
Related1JB3
DescriptorAgrin, CHLORIDE ION (2 entities in total)
Functional Keywordsneuromuscular junction, agrin, interaction coiled-doil proteins with globular proteins, ob-fold, timp, cell adhesion
Biological sourceGallus gallus (chicken)
Total number of polymer chains1
Total formula weight15182.80
Authors
Stetefeld, J. (deposition date: 2001-06-08, release date: 2001-08-08, Last modification date: 2024-10-30)
Primary citationStetefeld, 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: 11473262
DOI: 10.1038/90422
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.73 Å)
Structure validation

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