6SH2

Crystal structure of human neprilysin E584D in complex with C-type natriuretic peptide.

これはPDB形式変換不可エントリーです。

6SH2 の概要

• エントリーDOI: 10.2210/pdb6sh2/pdb
• 分子名称: Neprilysin, C-type natriuretic peptide fragment (CNP), 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total)
• 機能のキーワード: zinc metalloprotease, neprilysin, neutral endopeptidase., peptide binding protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 80834.95

構造登録者

Moss, S.,Subramanian, V.,Acharya, K.R. (登録日: 2019-08-05, 公開日: 2019-09-25, 最終更新日: 2024-10-16)

主引用文献

Moss, S.,Subramanian, V.,Acharya, K.R.
Crystal structure of peptide-bound neprilysin reveals key binding interactions.
Febs Lett., 594:327-336, 2020

PubMed Abstract: Neprilysin (NEP) is a promiscuous zinc metalloprotease with broad substrate specificity and cleaves a remarkable diversity of substrates through endopeptidase action. Two of these - amyloid-β and natriuretic peptides - implicate the enzyme in both Alzheimer's disease and cardiovascular disease, respectively. Here, we report the creation of a catalytically inactive NEP (E584D) to determine the first peptide-bound crystal structure at 2.6 Å resolution. The structure reveals key interactions involved in substrate binding which we have identified to be conserved in other known zinc metalloproteases. In addition, the structure provides evidence for a potential exosite within the central cavity that may play a critical role in substrate positioning. Together, these results contribute to our understanding of the molecular function of NEP.

PubMed: 31514225
DOI: 10.1002/1873-3468.13602

実験手法

X-RAY DIFFRACTION (2.6 Å)