1MCV

Crystal Structure Analysis of a Hybrid Squash Inhibitor in Complex with Porcine Pancreatic Elastase

1MCV の概要

• エントリーDOI: 10.2210/pdb1mcv/pdb
• 関連するPDBエントリー: 1PPE 1PPF 1QNJ
• 分子名称: Elastase 1, HEI-TOE I, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: elastase-inhibitor complex, hybrid squash inhibitor, hydrolase
• 由来する生物種: Sus scrofa (pig); 詳細
• 細胞内の位置: Secreted: P00772
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29038.61

構造登録者

Ay, J.,Hilpert, K.,Krauss, N.,Schneider-Mergener, J.,Hoehne, W. (登録日: 2002-08-06, 公開日: 2003-02-04, 最終更新日: 2024-11-13)

主引用文献

Ay, J.,Hilpert, K.,Krauss, N.,Schneider-Mergener, J.,Hohne, W.
Structure of a hybrid squash inhibitor in complex with porcine pancreatic elastase at 1.8 A resolution.
Acta Crystallogr.,Sect.D, 59:247-254, 2003

PubMed Abstract: The crystal structure of porcine pancreatic elastase in complex with a hybrid squash inhibitor (HEI-TOE I; 28 amino acids) has been determined to a resolution of 1.8 A. To construct the hybrid inhibitor, the trypsin-binding loop of the squash inhibitor from Ecballium elaterium was substituted by the sequence of a peptide that was derived from the third domain of the turkey ovomucoid inhibitor and was optimized to inhibit porcine pancreatic elastase. This modification of the squash inhibitor changed its specificity for trypsin to a specificity for porcine pancreatic elastase. Specific interactions of this hybrid inhibitor with porcine pancreatic elastase and the differences from the interactions of the ovomucoid inhibitor with human leukocyte elastase are discussed. The binding loop of the inhibitor adopts a 'canonical' conformation and the scissile bond Leu-Glu remains intact.

PubMed: 12554935
DOI: 10.1107/S0907444902020887

実験手法

X-RAY DIFFRACTION (1.8 Å)