3V64
Crystal Structure of agrin and LRP4
3V64 の概要
| エントリーDOI | 10.2210/pdb3v64/pdb |
| 関連するPDBエントリー | 3V65 |
| 分子名称 | Low-density lipoprotein receptor-related protein 4, Isoform 4 of Agrin, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| 機能のキーワード | beta propeller, laminin-g, signaling, protein binding |
| 由来する生物種 | Rattus norvegicus (Norway rat) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 121718.88 |
| 構造登録者 | |
| 主引用文献 | Zong, Y.,Zhang, B.,Gu, S.,Lee, K.,Zhou, J.,Yao, G.,Figueiredo, D.,Perry, K.,Mei, L.,Jin, R. Structural basis of agrin-LRP4-MuSK signaling. Genes Dev., 26:247-258, 2012 Cited by PubMed Abstract: Synapses are the fundamental units of neural circuits that enable complex behaviors. The neuromuscular junction (NMJ), a synapse formed between a motoneuron and a muscle fiber, has contributed greatly to understanding of the general principles of synaptogenesis as well as of neuromuscular disorders. NMJ formation requires neural agrin, a motoneuron-derived protein, which interacts with LRP4 (low-density lipoprotein receptor-related protein 4) to activate the receptor tyrosine kinase MuSK (muscle-specific kinase). However, little is known of how signals are transduced from agrin to MuSK. Here, we present the first crystal structure of an agrin-LRP4 complex, consisting of two agrin-LRP4 heterodimers. Formation of the initial binary complex requires the z8 loop that is specifically present in neuronal, but not muscle, agrin and that promotes the synergistic formation of the tetramer through two additional interfaces. We show that the tetrameric complex is essential for neuronal agrin-induced acetylcholine receptor (AChR) clustering. Collectively, these results provide new insight into the agrin-LRP4-MuSK signaling cascade and NMJ formation and represent a novel mechanism for activation of receptor tyrosine kinases. PubMed: 22302937DOI: 10.1101/gad.180885.111 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.85 Å) |
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