Journal
JOURNAL OF STRUCTURAL BIOLOGY
Volume 152, Issue 3, Pages 195-203Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.jsb.2005.09.006
Keywords
snake venom metalloprotemase; non-hemmorhagic; crystal structure; zinc binding; Agkistrodon acutus; fibrin/fibrinogen; thrombotic occlusive diseases
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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 a water molecule. Unambiguous electron density for a tripeptide 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. (C) 2005 Elsevier Inc. All rights reserved.
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