4OMC

X-ray structure of human furin in complex with the competitive inhibitor meta-guanidinomethyl-Phac-RVR-Amba

4OMC の概要

• エントリーDOI: 10.2210/pdb4omc/pdb
• 関連するPDBエントリー: 1P8J 4OMD
• 関連するBIRD辞書のPRD_ID: PRD_001220
• 分子名称: Furin, meta-guanidinomethyl-phenylacetyl-Arg-Val-Arg-(amidomethyl)benzamidine, FORMIC ACID, ... (6 entities in total)
• 機能のキーワード: pro-protein convertase, serine protease, competitive inhibitor, protease-inhibitor complex, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein: P09958
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 320807.11

構造登録者

Dahms, S.O.,Than, M.E. (登録日: 2014-01-27, 公開日: 2014-04-09, 最終更新日: 2024-11-27)

主引用文献

Dahms, S.O.,Hardes, K.,Becker, G.L.,Steinmetzer, T.,Brandstetter, H.,Than, M.E.
X-ray Structures of Human Furin in Complex with Competitive Inhibitors.
Acs Chem.Biol., 9:1113-1118, 2014

PubMed Abstract: Furin inhibitors are promising therapeutics for the treatment of cancer and numerous infections caused by bacteria and viruses, including the highly lethal Bacillus anthracis or the pandemic influenza virus. Development and improvement of inhibitors for pharmacological use require a detailed knowledge of the protease's substrate and inhibitor binding properties. Here we present a novel preparation of human furin and the first crystal structures of this enzyme in complex with noncovalent inhibitors. We show the inhibitor exchange by soaking, allowing the investigation of additional inhibitors and substrate analogues. Thus, our work provides a basis for the rational design of furin inhibitors.

PubMed: 24666235
DOI: 10.1021/cb500087x

実験手法

X-RAY DIFFRACTION (2.3 Å)