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- Title
Crystal structure of RVV-X: An example of evolutionary gain of specificity by ADAM proteinases
- Authors
Takeda, Soichi; Igarashi, Tomoko; Mori, Hidezo
- Abstract
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 2.9Å 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 6.5nm 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.
- Subjects
POISONOUS animals; NEUTRAL proteinases; PROTEINASES; PROTEOLYTIC enzymes
- Publication
FEBS Letters, 2007, Vol 581, Issue 30, p5859
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2007.11.062