3NYL

The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain

「1RW6」から置き換えられました

3NYL の概要

• エントリーDOI: 10.2210/pdb3nyl/pdb
• 関連するPDBエントリー: 1RW6 3NYJ
• 分子名称: Amyloid beta (A4) protein (Peptidase nexin-II, Alzheimer disease), isoform CRA_b (2 entities in total)
• 機能のキーワード: alzheimer's disease, helical hairpin, cell adhesion
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24735.11

構造登録者

Ha, Y.,Hu, J.,Lee, S.,Liu, X.,Wang, Y. (登録日: 2010-07-15, 公開日: 2011-07-13, 最終更新日: 2024-02-21)

主引用文献

Wang, Y.,Ha, Y.
The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain.
Mol.Cell, 15:343-353, 2004

PubMed Abstract: Amyloid beta-peptide, which forms neuronal and vascular amyloid deposits in Alzheimer's disease, is derived from an integral membrane protein precursor. The biological function of the precursor is currently unclear. Here we describe the X-ray structure of E2, the largest of the three conserved domains of the precursor. The structure of E2 consists of two coiled-coil substructures connected through a continuous helix and bears an unexpected resemblance to the spectrin family of protein structures. E2 can reversibly dimerize in the solution, and the dimerization occurs along the longest dimension of the molecule in an antiparallel orientation, which enables the N-terminal substructure of one monomer to pack against the C-terminal substructure of a second monomer. Heparan sulfate proteoglycans, the putative ligand for the precursor present in extracellular matrix, bind to E2 at a conserved and positively charged site near the dimer interface.

PubMed: 15304215
DOI: 10.1016/j.molcel.2004.06.037

実験手法

X-RAY DIFFRACTION (2.8 Å)