1ROA

Structure of human cystatin D

1ROA の概要

• エントリーDOI: 10.2210/pdb1roa/pdb
• 関連するPDBエントリー: 1RN7
• 分子名称: Cystatin D (2 entities in total)
• 機能のキーワード: inhibitor of cysteine pepidases, cystatin d, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Secreted : P28325
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13927.62

構造登録者

Alvarez-Fernandez, M.,Liang, Y.H.,Abrahamson, M.,Su, X.D. (登録日: 2003-12-01, 公開日: 2004-05-18, 最終更新日: 2024-10-30)

主引用文献

Alvarez-Fernandez, M.,Liang, Y.H.,Abrahamson, M.,Su, X.D.
Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile.
J.Biol.Chem., 280:18221-18228, 2005

PubMed Abstract: Cystatins are natural inhibitors of papain-like (family C1) and legumain-related (family C13) cysteine peptidases. Cystatin D is a type 2 cystatin, a secreted inhibitor found in human saliva and tear fluid. Compared with its homologues, cystatin D presents an unusual inhibition profile with a preferential inhibition cathepsin S > cathepsin H > cathepsin L and no inhibition of cathepsin B or pig legumain. To elucidate the structural reasons for this specificity, we have crystallized recombinant human Arg(26)-cystatin D and solved its structures at room temperature and at cryo conditions to 2.5- and 1.8-A resolution, respectively. Human cystatin D presents the typical cystatin fold, with a five-stranded anti-parallel beta-sheet wrapped around a five-turn alpha-helix. The structures reveal differences in the peptidase-interacting regions when compared with other cystatins, providing plausible explanations for the restricted inhibitory specificity of cystatin D for some papain-like peptidases and its lack of reactivity toward legumain-related enzymes.

PubMed: 15728581
DOI: 10.1074/jbc.M411914200

実験手法

X-RAY DIFFRACTION (1.8 Å)