7Z9F

Human anionic trypsin after autoproteolysis at Arg122

7Z9F の概要

• エントリーDOI: 10.2210/pdb7z9f/pdb
• 分子名称: Trypsin-2, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: try2, serine protease, autoproteolysis, digestion, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 48237.86

構造登録者

Nagel, F.,Palm, G.J.,Delcea, M.,Lammers, M. (登録日: 2022-03-21, 公開日: 2022-06-29, 最終更新日: 2024-10-09)

主引用文献

Nagel, F.,Susemihl, A.,Geist, N.,Mohlis, K.,Palm, G.J.,Lammers, M.,Delcea, M.
Structural Basis of the Pancreatitis-Associated Autoproteolytic Failsafe Mechanism in Human Anionic Trypsin.
J Inflamm Res, 15:3633-3642, 2022

PubMed Abstract: The pathophysiological mechanisms underlying chronic pancreatitis (CP) are still poorly understood. Human cationic (TRY1) and anionic (TRY2) trypsins are the two major trypsin isoforms and their activities are tightly regulated within pancreatic acinar cells. Typically, they exist in a molar ratio of 2:1 (cationic:anionic). This ratio is reversed during chronic alcohol abuse, pancreatic cancer, or pancreatitis due to selectively upregulated expression of TRY2, causing anionic trypsin to become the predominant isoform. The involvement of TRY2 in pancreatitis is considered limited due to the absence of disease-causing mutations and its increased prevalence for autoproteolysis. However, exacerbated pancreatitis in TRY2 overexpressing mice was recently demonstrated. Here, we aim to elucidate the molecular structure of human anionic trypsin and obtain insights into the autoproteolytic regulation of tryptic activity.

PubMed: 35775010
DOI: 10.2147/JIR.S367699

実験手法

X-RAY DIFFRACTION (1.7 Å)