2CIO

The high resolution x-ray structure of papain complexed with fragments of the Trypanosoma brucei cysteine protease inhibitor ICP.

2CIO の概要

• エントリーDOI: 10.2210/pdb2cio/pdb
• 関連するPDBエントリー: 1BP4 1BQI 1CVZ 1EFF 1KHP 1KHQ 1PAD 1PE6 1PIP 1POP 1PPD 1PPN 1PPP 1STF 2PAD 4PAD 5PAD 6PAD 9PAP
• 分子名称: PAPAIN, INHIBITOR OF CYSTEINE PEPTIDASE, GLYCEROL, ... (5 entities in total)
• 機能のキーワード: hydrolase/inhibitor, complex hydrolase-inhibitor, icp, cysteine protease, inhibitor, trypanosoma brucei, allergen, protease, thiol protease, zymogen, hydrolase, hydrolase-inhibitor complex
• 由来する生物種: TRYPANOSOMA BRUCEI; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 37309.84

構造登録者

Alphey, M.S.,Hunter, W.N. (登録日: 2006-03-24, 公開日: 2006-05-18, 最終更新日: 2023-12-13)

主引用文献

Alphey, M.S.,Hunter, W.N.
High-Resolution Complex of Papain with Remnants of a Cysteine Protease Inhibitor Derived from Trypanosoma Brucei
Acta Crystallogr.,Sect.F, 62:504-, 2006

PubMed Abstract: Attempts to cocrystallize the cysteine protease papain derived from the latex of Carica papaya with an inhibitor of cysteine proteases (ICP) from Trypanosoma brucei were unsuccessful. However, crystals of papain that diffracted to higher resolution, 1.5 A, than other crystals of this archetypal cysteine protease were obtained, so the analysis was continued. Surprisingly, the substrate-binding cleft was occupied by two short peptide fragments which have been assigned as remnants of ICP. Comparisons reveal that these peptides bind in the active site in a manner similar to that of the human cysteine protease inhibitor stefin B when it is complexed to papain. The assignment of the fragment sequences is consistent with the specificity of the protease.

PubMed: 16754967
DOI: 10.1107/S1744309106014849

実験手法

X-RAY DIFFRACTION (1.5 Å)