Activation of Factor X by Snake Venom Proteases

  • Jüri SiigurEmail author
  • Ene Siigur


Human coagulation factor X is a serine protease zymogen, which circulates in blood as a two-chain molecule. A variety of factor X activators have been detected in snake venoms. About 15 activators have been isolated from Viperidae, Crotalidae and Elapidae venoms. Viperidae and Crotalidae venom activators are mainly metalloproteases. Only two factor X activators are characterized from Elapidae venoms, both belonging to serine proteases. Most thoroughly investigated snake venom factor X activators are from Vipera russellii (now renamed Daboia russellii) - RVV-X, and Vipera lebetina (now renamed Macrovipera lebetina) - VLFXA. RVV-X is a heterotrimeric metalloproteinase with a mammalian ADAM-like heavy chain and two lectin-like light chains. The crystal structure of RVV-X has recently been determined. VLFXA is the first factor X activator that was cloned and sequenced and its primary structure was deduced from the cDNA sequences. Both activators consist of a heavy chain and two C-type lectin–like light chains which are held together by disulfide bonds. Heavy chains of RVV-X and VLFXA contain metalloprotease, disintegrin-like and cysteine-rich domains. All chains of VLFXA and RVV-X are synthesized from different genes. The primary structures of factor X activating snake venom serine proteases are unknown up to now.


Light Chain Heavy Chain Sialic Acid Snake Venom Tenase Complex 
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The work was financially supported by Estonian Science Foundation grant No. 7251 and by target financing SF0180114Bs08.


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© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  1. 1.Laboratory of Bioorganic ChemistryNational Institute of Chemical Physics and BiophysicsTallinnEstonia
  2. 2.National Institute of Chemical Physics and BiophysicsTallinnEstonia

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