Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050476 | FEBS Letters | 2007 | 6 Pages |
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.
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Soichi Takeda, Tomoko Igarashi, Hidezo Mori,