5ONR

Alzheimer's Amyloid-Beta Peptide Fragment 1-40 in Complex with Thermolysin

5ONR の概要

• エントリーDOI: 10.2210/pdb5onr/pdb
• 関連するPDBエントリー: 5ONP 5ONQ
• 分子名称: Thermolysin, Amyloid-beta A4 protein, CALCIUM ION, ... (6 entities in total)
• 機能のキーワード: peptidase, protein-peptide complex, amyloid-beta peptide, hydrolase
• 由来する生物種: Bacillus thermoproteolyticus; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 34965.57

構造登録者

Leite, J.P.,Gales, L. (登録日: 2017-08-04, 公開日: 2018-08-29, 最終更新日: 2024-01-17)

主引用文献

Leite, J.P.,Gales, L.
Alzheimer's A beta1-40peptide degradation by thermolysin: evidence of inhibition by a C-terminal A beta product.
FEBS Lett., 593:128-137, 2019

PubMed Abstract: The interaction of the amyloid-β peptide (Aβ) with thermolysin (TLN) was investigated by X-ray crystallography. Structural models of the complexes of TLN with several Aβ fragments show that, despite the numerous possible cleavage sites of the Aβ sequence, the C-terminal product of Ala30-Ile31 cleavage does not dissociate, thus inhibiting the enzyme. The high similarity between the TLN structural motif and neprilysin (NEP), the most extensively studied peptidase associated with Aβ clearance, suggests that NEP should be more efficient against Aβ polymorphs where Ala30-Ile31 is inaccessible, which is in agreement with studies in living mice that point to the limited role of NEP in degrading soluble Aβ and its higher ability to degrade insoluble and/or oligomeric Aβ forms, producing only the Aβ intermediate.

PubMed: 30403288
DOI: 10.1002/1873-3468.13285

実験手法

X-RAY DIFFRACTION (1.39 Å)