1JB3

The Laminin-Binding Domain of Agrin is structurally related to N-TIMP-1

1JB3 の概要

• エントリーDOI: 10.2210/pdb1jb3/pdb
• 分子名称: Agrin (2 entities in total)
• 機能のキーワード: neuromuscular junction, agrin, interaction coiled-doil proteins with globular proteins, ob-fold, timp, cell adhesion
• 由来する生物種: Gallus gallus (chicken)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15131.32

構造登録者

Stetefeld, J. (登録日: 2001-06-01, 公開日: 2001-08-08, 最終更新日: 2024-02-07)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.6 Å)