5V65

Crystal structure of macrocycles containing Abeta 17-23 (LV(PHI)FAED) and Abeta 30-36 (AII(SAR)L(ORN)V)

5V65 の概要

• エントリーDOI: 10.2210/pdb5v65/pdb
• 関連するPDBエントリー: 5V63 5V64
• 分子名称: ORN-LEU-VAL-PHI-PHE-ALA-GLU-ASP-ORN-ALA-ILE-ILE-SAR-LEU-MET-VAL (2 entities in total)
• 機能のキーワード: beta-hairpin, macrocycle, de novo protein
• 由来する生物種: synthetic construct
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 30497.20

構造登録者

Kreutzer, A.G.,Salveson, P.J.,Nowick, J.S. (登録日: 2017-03-15, 公開日: 2017-06-28, 最終更新日: 2025-04-02)

主引用文献

Salveson, P.J.,Spencer, R.K.,Kreutzer, A.G.,Nowick, J.S.
X-ray Crystallographic Structure of a Compact Dodecamer from a Peptide Derived from A beta 16-36.
Org. Lett., 19:3462-3465, 2017

PubMed Abstract: The assembly of the β-amyloid peptide, Aβ, into soluble oligomers is associated with neurodegeneration in Alzheimer's disease. The Aβ oligomers are thought to be composed of β-hairpins. Here, the effect of shifting the residue pairing of the β-hairpins on the structures of the oligomers that form is explored through X-ray crystallography. Three residue pairings were investigated using constrained macrocyclic β-hairpins in which Aβ is juxtaposed with Aβ, Aβ, and Aβ. The Aβ-Aβ pairing forms a compact ball-shaped dodecamer composed of fused triangular trimers. This dodecamer may help explain the structures of the trimers and dodecamers formed by full-length Aβ.

PubMed: 28683555
DOI: 10.1021/acs.orglett.7b01445

実験手法

X-RAY DIFFRACTION (2.52 Å)