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5XWU

Crystal structure of PTPdelta Ig1-Ig3 in complex with SALM2 LRR-Ig

5XWU の概要
エントリーDOI10.2210/pdb5xwu/pdb
分子名称Receptor-type tyrosine-protein phosphatase delta, Leucine-rich repeat and fibronectin type III domain-containing protein 1, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
機能のキーワードsynaptic orgnizers, cell adhesion
由来する生物種Mus musculus (Mouse)
詳細
タンパク質・核酸の鎖数4
化学式量合計151924.35
構造登録者
Goto-Ito, S.,Yamagata, A.,Sato, Y.,Fukai, S. (登録日: 2017-06-30, 公開日: 2018-06-06, 最終更新日: 2024-10-23)
主引用文献Goto-Ito, S.,Yamagata, A.,Sato, Y.,Uemura, T.,Shiroshima, T.,Maeda, A.,Imai, A.,Mori, H.,Yoshida, T.,Fukai, S.
Structural basis of trans-synaptic interactions between PTP delta and SALMs for inducing synapse formation.
Nat Commun, 9:269-269, 2018
Cited by
PubMed Abstract: Synapse formation is triggered by trans-synaptic interactions of cell adhesion molecules, termed synaptic organizers. Three members of type-II receptor protein tyrosine phosphatases (classified as type-IIa RPTPs; PTPδ, PTPσ and LAR) are known as presynaptic organizers. Synaptic adhesion-like molecules (SALMs) have recently emerged as a family of postsynaptic organizers. Although all five SALM isoforms can bind to the type-IIa RPTPs, only SALM3 and SALM5 reportedly have synaptogenic activities depending on their binding. Here, we report the crystal structures of apo-SALM5, and PTPδ-SALM2 and PTPδ-SALM5 complexes. The leucine-rich repeat (LRR) domains of SALMs interact with the second immunoglobulin-like (Ig) domain of PTPδ, whereas the Ig domains of SALMs interact with both the second and third Ig domains of PTPδ. Unexpectedly, the structures exhibit the LRR-mediated 2:2 complex. Our synaptogenic co-culture assay using site-directed SALM5 mutants demonstrates that presynaptic differentiation induced by PTPδ-SALM5 requires the dimeric property of SALM5.
PubMed: 29348429
DOI: 10.1038/s41467-017-02417-z
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.162 Å)
構造検証レポート
Validation report summary of 5xwu
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-04-02に公開中

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