1YP1

Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase from venom of Agkistrodon acutus

1YP1 の概要

• エントリーDOI: 10.2210/pdb1yp1/pdb
• 分子名称: FII, KNL, ZINC ION, ... (4 entities in total)
• 機能のキーワード: fii crystal structure, hydrolase
• 由来する生物種: Deinagkistrodon acutus (Chinese moccasin); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22427.22

構造登録者

Lou, Z.,Hou, J.,Chen, J.,Liang, X.,Qiu, P.,Liu, Y.,Li, M.,Rao, Z. (登録日: 2005-01-28, 公開日: 2006-01-17, 最終更新日: 2024-10-16)

主引用文献

Lou, Z.,Hou, J.,Liang, X.,Chen, J.,Qiu, P.,Liu, Y.,Li, M.,Rao, Z.,Yan, G.
Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase complexed with a novel natural tri-peptide inhibitor from venom of Agkistrodon acutus
J.Struct.Biol., 152:195-203, 2005

PubMed Abstract: Thrombotic occlusive diseases pose a great threat to human health. Thrombolytic agents are in widespread use for the dissolution of arterial and venous pathologic thrombi in these kinds of diseases. Snake venom metalloproteinases (SVMPs) can act directly on fibrin/fibrinogen and are therefore potential candidates for therapeutic use against thrombotic occlusive diseases. In this study, we have determined the crystal structure of FII, a novel non-hemorrhagic SVMP isolated from Anhui Agkistrodon acutus snake venom by molecular replacement. The structure reveals that FII is a member of the P-I class SVMPs. The Zn2+ ion essential for hydrolytic activity is found in the active site and is tetrahedrally co-ordinated by three histidine residues and water molecule. Unambiguous electron density for a tri-peptide with sequence KNL is also found located near the active site. Biochemical evidences show that the tri-peptide KNL can inhibit the enzymatic activity of FII.

PubMed: 16330227
DOI: 10.1016/j.jsb.2005.09.006

実験手法

X-RAY DIFFRACTION (1.9 Å)