8PCH

CRYSTAL STRUCTURE OF PORCINE CATHEPSIN H DETERMINED AT 2.1 ANGSTROM RESOLUTION: LOCATION OF THE MINI-CHAIN C-TERMINAL CARBOXYL GROUP DEFINES CATHEPSIN H AMINOPEPTIDASE FUNCTION

8PCH の概要

• エントリーDOI: 10.2210/pdb8pch/pdb
• 分子名称: CATHEPSIN H, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
• 機能のキーワード: hydrolase, protease, cysteine proteinase, aminopeptidase
• 由来する生物種: Sus scrofa (pig); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 25763.94

構造登録者

Guncar, G.,Podobnik, M.,Pungercar, J.,Strukelj, B.,Turk, V.,Turk, D. (登録日: 1997-11-07, 公開日: 1998-12-09, 最終更新日: 2024-11-13)

主引用文献

Guncar, G.,Podobnik, M.,Pungercar, J.,Strukelj, B.,Turk, V.,Turk, D.
Crystal structure of porcine cathepsin H determined at 2.1 A resolution: location of the mini-chain C-terminal carboxyl group defines cathepsin H aminopeptidase function.
Structure, 6:51-61, 1998

PubMed Abstract: Cathepsin H is a lysosomal cysteine protease, involved in intracellular protein degradation. It is the only known mono-aminopeptidase in the papain-like family and is reported to be involved in tumor metastasis. The cathepsin H structure was determined in order to investigate the structural basis for its aminopeptidase activity and thus to provide the basis for structure-based design of synthetic inhibitors.

PubMed: 9493267
DOI: 10.1016/S0969-2126(98)00007-0

実験手法

X-RAY DIFFRACTION (2.1 Å)