Crystal structure of RVV‐X: An example of evolutionary gain of specificity by ADAM proteinases

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Abstract
Russell's viper venom factor X activator (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 been determined at 2.9 Å resolution and shows a hook‐spanner‐wrench‐like architecture, in which the metalloproteinase/disintegrin region constitutes a hook, and the lectin‐like domains constitute a handle. A 6.5 nm separation between the catalytic site and a putative exosite suggests a docking model for factor X. The structure provides a typical example of the molecular evolution of multi‐subunit proteins and insights into the molecular basis of target recognition and proteolysis by ADAM/adamalysin/reprolysin proteinases.

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