3PXJ

Tandem Ig repeats of Dlar

3PXJ の概要

• エントリーDOI: 10.2210/pdb3pxj/pdb
• 関連するPDBエントリー: 3PX4
• 分子名称: Tyrosine-protein phosphatase Lar (2 entities in total)
• 機能のキーワード: ig domains, cell adhesion, receptor protein tyrosine phosphatase, hydrolase
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Membrane; Single-pass type I membrane protein: P16621
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 90970.49

構造登録者

Biersmith, B.H.,Bouyain, S. (登録日: 2010-12-10, 公開日: 2011-03-23, 最終更新日: 2024-10-30)

主引用文献

Biersmith, B.H.,Hammel, M.,Geisbrecht, E.R.,Bouyain, S.
The Immunoglobulin-like Domains 1 and 2 of the Protein Tyrosine Phosphatase LAR Adopt an Unusual Horseshoe-like Conformation.
J.Mol.Biol., 408:616-627, 2011

PubMed Abstract: Neurogenesis depends on exquisitely regulated interactions between macromolecules on the cell surface and in the extracellular matrix. In particular, interactions between proteoglycans and members of the type IIa subgroup of receptor protein tyrosine phosphatases underlie crucial developmental processes such as the formation of synapses at the neuromuscular junction and the migration of axons to their appropriate targets. We report the crystal structures of the first and second immunoglobulin-like domains of the Drosophila type IIa receptor Dlar and its mouse homolog LAR. These two domains adopt an unusual antiparallel arrangement that has not been reported in tandem repeats of immunoglobulin-like domains and that is presumably conserved in all type IIa receptor protein tyrosine phosphatases.

PubMed: 21402080
DOI: 10.1016/j.jmb.2011.03.013

実験手法

X-RAY DIFFRACTION (2.3003 Å)