Structural highlights
Evolutionary Conservation
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Publication Abstract from PubMed
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.
Crystal structure of a non-hemorrhagic fibrin(ogen)olytic metalloproteinase complexed with a novel natural tri-peptide inhibitor from venom of Agkistrodon acutus.,Lou Z, Hou J, Liang X, Chen J, Qiu P, Liu Y, Li M, Rao Z, Yan G J Struct Biol. 2005 Dec;152(3):195-203. Epub 2005 Nov 16. PMID:16330227[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. 2005 Dec;152(3):195-203. Epub 2005 Nov 16. PMID:16330227 doi:10.1016/j.jsb.2005.09.006
