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Structural Aspects of the Factor X Activator RVV-X from Russell’s Viper Venom

  • Soichi TakedaEmail author
Chapter

Abstract

The venom of Russell’s viper Daboia russelli contains a potent blood coagulation factor X activator, RVV-X. Because of its high specificity, RVV-X is widely used in laboratories and as a diagnostic tool. RVV-X is a unique heterotrimeric metalloproteinase containing a mammalian a disintegrin and metalloproteinase (ADAM)-like heavy chain and two C-type lectin-like light chains, which are covalently held together by disulfide bonds. The crystal structure of RVV-X indicates that RVV-X adopts a “hook-spanner-wrench”–like structure, in which the metalloproteinase/disintegrin portion constitutes a mobile hook and the lectin-like domains, together with the remainder of the heavy chain, constitute a handle. The lectin-like domains form an intertwined dimer with high structural similarity to anticoagulant factor X-binding proteins. The RVV-X structure displayed a 6.5-nm separation between the catalytic zinc atom and a putative gamma carboxylglutamic acid (Gla) domain–binding exosite, implying molecular mechanism of factor X activation by RVV-X. The three-dimensional structure of RVV-X also provides a typical example of the molecular evolution of protein complexes, giving insight into the molecular basis of substrate recognition and proteolysis by adamalysin/reprolysin/ADAM family proteinases.

Keywords

Light Chain Snake Venom Serine Proteinase Domain Epidermal Growth Factor Domain ADAMTS Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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© Springer Science+Business Media B.V. 2010

Authors and Affiliations

  1. 1.National Cerebral and Cardiovascular Center Research InstituteSuitaJapan

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