1C4R

THE STRUCTURE OF THE LIGAND-BINDING DOMAIN OF NEUREXIN 1BETA: REGULATION OF LNS DOMAIN FUNCTION BY ALTERNATIVE SPLICING

1C4R の概要

• エントリーDOI: 10.2210/pdb1c4r/pdb
• 分子名称: NEUREXIN-I BETA (2 entities in total)
• 機能のキーワード: lectin-like, neurobiology, cell-cell adhesion, cell-cell recognition, alternative splicing, membrane protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Membrane; Single-pass type I membrane protein (Potential): Q63373
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 157544.58

構造登録者

Rudenko, G.,Nguyen, T.,Chelliah, Y.,Sudhof, T.C.,Deisenhofer, J. (登録日: 1999-09-28, 公開日: 2000-10-04, 最終更新日: 2023-12-27)

主引用文献

Rudenko, G.,Nguyen, T.,Chelliah, Y.,Sudhof, T.C.,Deisenhofer, J.
The structure of the ligand-binding domain of neurexin Ibeta: regulation of LNS domain function by alternative splicing.
Cell(Cambridge,Mass.), 99:93-101, 1999

PubMed Abstract: Neurexins are expressed in hundreds of isoforms on the neuronal cell surface, where they may function as cell recognition molecules. Neurexins contain LNS domains, folding units found in many proteins like the G domain of laminin A, agrin, and slit. The crystal structure of neurexin Ibeta, a single LNS domain, reveals two seven-stranded beta sheets forming a jelly roll fold with unexpected structural similarity to lectins. The LNS domains of neurexin and agrin undergo alternative splicing that modulates their affinity for protein ligands in a neuron-specific manner. These splice sites are localized within loops at one edge of the jelly roll, suggesting a distinct protein interaction surface in LNS domains that is regulated by alternative splicing.

PubMed: 10520997
DOI: 10.1016/S0092-8674(00)80065-3

実験手法

X-RAY DIFFRACTION (2.6 Å)