1PZ7

Modulation of agrin function by alternative splicing and Ca2+ binding

1PZ7 の概要

• エントリーDOI: 10.2210/pdb1pz7/pdb
• 関連するPDBエントリー: 1Q56
• 分子名称: Agrin, CALCIUM ION (3 entities in total)
• 機能のキーワード: agrin, structural protein
• 由来する生物種: Gallus gallus (chicken)
• 細胞内の位置: Secreted, extracellular space, extracellular matrix: P31696
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44770.74

構造登録者

Stetefeld, J.,Alexandrescu, A.T.,Maciejewski, M.W.,Jenny, M.,Rathgeb-Szabo, K.,Schulthess, T.,Landwehr, R.,Frank, S.,Ruegg, M.A.,Kammerer, R.A. (登録日: 2003-07-10, 公開日: 2004-04-13, 最終更新日: 2024-11-13)

主引用文献

Stetefeld, J.,Alexandrescu, A.T.,Maciejewski, M.W.,Jenny, M.,Rathgeb-Szabo, K.,Schulthess, T.,Landwehr, R.,Frank, S.,Ruegg, M.A.,Kammerer, R.A.
Modulation of agrin function by alternative splicing and Ca2+ binding.
STRUCTURE, 12:503-515, 2004

PubMed Abstract: The aggregation of acetylcholine receptors on postsynaptic membranes is a key step in neuromuscular junction development. This process depends on alternatively spliced forms of the proteoglycan agrin with "B-inserts" of 8, 11, or 19 residues in the protein's globular C-terminal domain, G3. Structures of the neural B8 and B11 forms of agrin-G3 were determined by X-ray crystallography. The structure of G3-B0, which lacks inserts, was determined by NMR. The agrin-G3 domain adopts a beta jellyroll fold. The B insert site is flanked by four loops on one edge of the beta sandwich. The loops form a surface that corresponds to a versatile interaction interface in the family of structurally related LNS proteins. NMR and X-ray data indicate that this interaction interface is flexible in agrin-G3 and that flexibility is reduced by Ca(2+) binding. The plasticity of the interaction interface could enable different splice forms of agrin to select between multiple binding partners.

PubMed: 15016366
DOI: 10.1016/j.str.2004.02.001

実験手法

X-RAY DIFFRACTION (1.421 Å)